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Protein

Myosin heavy chain, skeletal muscle, adult

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi180 – 187ATPSequence analysis8

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin heavy chain, skeletal muscle, adult
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001234342 – 1939Myosin heavy chain, skeletal muscle, adultAdd BLAST1938

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei36N6-methyllysine1 Publication1
Modified residuei131N6,N6,N6-trimethyllysine1 Publication1
Modified residuei552N6,N6,N6-trimethyllysine1 Publication1
Modified residuei756Pros-methylhistidine1 Publication1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP13538.
PRIDEiP13538.

PTM databases

iPTMnetiP13538.

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).

Protein-protein interaction databases

STRINGi9031.ENSGALP00000001425.

Structurei

Secondary structure

11939
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 18Combined sources4
Turni22 – 25Combined sources4
Helixi26 – 29Combined sources4
Turni35 – 37Combined sources3
Beta strandi38 – 42Combined sources5
Beta strandi44 – 56Combined sources13
Beta strandi58 – 63Combined sources6
Beta strandi66 – 68Combined sources3
Beta strandi71 – 74Combined sources4
Helixi75 – 77Combined sources3
Beta strandi86 – 88Combined sources3
Helixi92 – 94Combined sources3
Helixi100 – 109Combined sources10
Turni110 – 114Combined sources5
Beta strandi117 – 119Combined sources3
Beta strandi124 – 127Combined sources4
Helixi134 – 136Combined sources3
Helixi140 – 143Combined sources4
Turni144 – 146Combined sources3
Helixi156 – 170Combined sources15
Beta strandi174 – 180Combined sources7
Helixi186 – 200Combined sources15
Helixi219 – 234Combined sources16
Beta strandi242 – 245Combined sources4
Beta strandi247 – 255Combined sources9
Beta strandi257 – 263Combined sources7
Beta strandi266 – 269Combined sources4
Helixi273 – 276Combined sources4
Helixi287 – 292Combined sources6
Helixi298 – 304Combined sources7
Helixi310 – 312Combined sources3
Helixi314 – 316Combined sources3
Helixi328 – 341Combined sources14
Helixi346 – 362Combined sources17
Beta strandi367 – 369Combined sources3
Beta strandi376 – 379Combined sources4
Helixi383 – 391Combined sources9
Helixi395 – 403Combined sources9
Beta strandi410 – 412Combined sources3
Helixi420 – 449Combined sources30
Beta strandi458 – 466Combined sources9
Beta strandi472 – 474Combined sources3
Helixi476 – 506Combined sources31
Helixi518 – 528Combined sources11
Helixi533 – 540Combined sources8
Helixi548 – 559Combined sources12
Beta strandi563 – 567Combined sources5
Beta strandi579 – 583Combined sources5
Beta strandi588 – 591Combined sources4
Helixi596 – 601Combined sources6
Helixi606 – 613Combined sources8
Helixi618 – 623Combined sources6
Helixi651 – 666Combined sources16
Beta strandi668 – 676Combined sources9
Helixi689 – 699Combined sources11
Helixi701 – 708Combined sources8
Beta strandi715 – 717Combined sources3
Helixi718 – 725Combined sources8
Helixi726 – 728Combined sources3
Turni729 – 731Combined sources3
Helixi743 – 748Combined sources6
Beta strandi751 – 753Combined sources3
Beta strandi756 – 762Combined sources7
Beta strandi765 – 768Combined sources4
Helixi772 – 827Combined sources56
Helixi831 – 839Combined sources9
Turni840 – 842Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-A1-844[»]
1M8Qelectron microscopy70.00A/D/G/P5-844[»]
1MVWelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O18electron microscopy70.00A/D/G/J/M/P5-844[»]
1O19electron microscopy70.00A/D/G/J/M/S5-844[»]
1O1Aelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Belectron microscopy70.00A/D/G/J5-844[»]
1O1Celectron microscopy70.00A/D/G/J/P5-844[»]
1O1Delectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Eelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Felectron microscopy70.00A/D/G/J5-844[»]
1O1Gelectron microscopy70.00A/D/G/J/M/P5-844[»]
2MYSX-ray2.80A2-844[»]
2W4Aelectron microscopy35.00M5-844[»]
2W4Gelectron microscopy35.00M5-844[»]
2W4Helectron microscopy35.00M5-844[»]
ProteinModelPortaliP13538.
SMRiP13538.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13538.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 781Myosin motorAdd BLAST695
Domaini784 – 813IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni658 – 680Actin-bindingAdd BLAST23
Regioni760 – 774Actin-bindingAdd BLAST15
Regioni839 – 841Hinge3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili842 – 1939Sequence analysisAdd BLAST1098

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

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOVERGENiHBG004704.
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.
[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.

P13538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPDAEMAA FGEAAPYLRK SEKERIEAQN KPFDAKSSVF VVHPKESFVK
60 70 80 90 100
GTIQSKEGGK VTVKTEGGET LTVKEDQVFS MNPPKYDKIE DMAMMTHLHE
110 120 130 140 150
PAVLYNLKER YAAWMIYTYS GLFCVTVNPY KWLPVYNPEV VLAYRGKKRQ
160 170 180 190 200
EAPPHIFSIS DNAYQFMLTD RENQSILITG ESGAGKTVNT KRVIQYFATI
210 220 230 240 250
AASGEKKKEE QSGKMQGTLE DQIISANPLL EAFGNAKTVR NDNSSRFGKF
260 270 280 290 300
IRIHFGATGK LASADIETYL LEKSRVTFQL PAERSYHIFY QIMSNKKPEL
310 320 330 340 350
IDMLLITTNP YDYHYVSQGE ITVPSIDDQE ELMATDSAID ILGFSADEKT
360 370 380 390 400
AIYKLTGAVM HYGNLKFKQK QREEQAEPDG TEVADKAAYL MGLNSAELLK
410 420 430 440 450
ALCYPRVKVG NEFVTKGQTV SQVHNSVGAL AKAVYEKMFL WMVIRINQQL
460 470 480 490 500
DTKQPRQYFI GVLDIAGFEI FDFNSFEQLC INFTNEKLQQ FFNHHMFVLE
510 520 530 540 550
QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE CMFPKATDTS
560 570 580 590 600
FKNKLYDQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNISGWLEKN
610 620 630 640 650
KDPLNETVIG LYQKSSVKTL ALLFATYGGE AEGGGGKKGG KKKGSSFQTV
660 670 680 690 700
SALFRENLNK LMANLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG
710 720 730 740 750
VLEGIRICRK GFPSRVLYAD FKQRYRVLNA SAIPEGQFMD SKKASEKLLG
760 770 780 790 800
SIDVDHTQYR FGHTKVFFKA GLLGLLEEMR DDKLAEIITR TQARCRGFLM
810 820 830 840 850
RVEYRRMVER RESIFCIQYN VRSFMNVKHW PWMKLFFKIK PLLKSAESEK
860 870 880 890 900
EMANMKEEFE KTKEELAKSE AKRKELEEKM VVLLQEKNDL QLQVQAEADS
910 920 930 940 950
LADAEERCDQ LIKTKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC
960 970 980 990 1000
SELKKDIDDL ELTLAKVEKE KHATENKVKN LTEEMAVLDE TIAKLTKEKK
1010 1020 1030 1040 1050
ALQEAHQQTL DDLQVEEDKV NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD
1060 1070 1080 1090 1100
LERAKRKLEG DLKLAHDSIM DLENDKQQLD EKLKKKDFEI SQIQSKIEDE
1110 1120 1130 1140 1150
QALGMQLQKK IKELQARIEE LEEEIEAERT SRAKAEKHRA DLSRELEEIS
1160 1170 1180 1190 1200
ERLEEAGGAT AAQIEMNKKR EAEFQKMRRD LEEATLQHEA TAAALRKKHA
1210 1220 1230 1240 1250
DSTAELGEQI DNLQRVKQKL EKEKSELKME IDDLASNMES VSKAKANLEK
1260 1270 1280 1290 1300
MCRTLEDQLS EIKTKEEQNQ RMINDLNTQR ARLQTETGEY SRQAEEKDAL
1310 1320 1330 1340 1350
ISQLSRGKQG FTQQIEELKR HLEEEIKAKN ALAHALQSAR HDCELLREQY
1360 1370 1380 1390 1400
EEEQEAKGEL QRALSKANSE VAQWRTKYET DAIQRTEELE EAKKKLAQRL
1410 1420 1430 1440 1450
QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMVDVERSNA ACAALDKKQK
1460 1470 1480 1490 1500
NFDKILAEWK QKYEETQTEL EASQKESRSL STELFKMKNA YEESLDHLET
1510 1520 1530 1540 1550
LKRENKNLQQ EIADLTEQIA EGGKAVHELE KVKKHVEQEK SELQASLEEA
1560 1570 1580 1590 1600
EASLEHEEGK ILRLQLELNQ IKSEIDRKIA EKDEEIDQLK RNHLRIVESM
1610 1620 1630 1640 1650
QSTLDAEIRS RNEALRLKKK MEGDLNEMEI QLSHANRMAA EAQKNLRNTQ
1660 1670 1680 1690 1700
GTLKDTQIHL DDALRTQEDL KEQVAMVERR ANLLQAEVEE LRGALEQTER
1710 1720 1730 1740 1750
SRKVAEQELL DATERVQLLH TQNTSLINTK KKLETDIVQI QSEMEDTIQE
1760 1770 1780 1790 1800
ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNMD QTVKDLHVRL
1810 1820 1830 1840 1850
DEAEQLALKG GKKQLQKLEA RVRELEGEVD SEQKRSAEAV KGVRKYERRV
1860 1870 1880 1890 1900
KELTYQCEED RKNILRLQDL VDKLQMKVKS YKRQAEEAEE LSNVNLSKFR
1910 1920 1930
KIQHELEEAE ERADIAESQV NKLRVKSREI HGKKIEEEE
Length:1,939
Mass (Da):223,145
Last modified:January 23, 2007 - v4
Checksum:iF6DAD73CABD82BFD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti908C → Q AA sequence (PubMed:2610940).Curated1
Sequence conflicti908C → Q AA sequence (PubMed:2775482).Curated1
Sequence conflicti981L → F in AAB47555 (PubMed:9358064).Curated1
Sequence conflicti1344E → D AA sequence (PubMed:1939030).Curated1
Sequence conflicti1546S → A AA sequence (PubMed:1939030).Curated1
Sequence conflicti1797 – 1798HV → QL AA sequence (PubMed:1939030).Curated2
Sequence conflicti1831S → A AA sequence (PubMed:1939030).Curated1
Sequence conflicti1864I → V in AAA48970 (PubMed:3034534).Curated1
Sequence conflicti1930 – 1932IHG → FH in AAA48970 (PubMed:3034534).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87231 mRNA. Translation: AAB47555.1.
M16557 Genomic DNA. Translation: AAA48970.1.
RefSeqiNP_001013415.1. NM_001013397.2.
UniGeneiGga.40396.
Gga.51379.

Genome annotation databases

GeneIDi427788.
KEGGigga:427788.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87231 mRNA. Translation: AAB47555.1.
M16557 Genomic DNA. Translation: AAA48970.1.
RefSeqiNP_001013415.1. NM_001013397.2.
UniGeneiGga.40396.
Gga.51379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-A1-844[»]
1M8Qelectron microscopy70.00A/D/G/P5-844[»]
1MVWelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O18electron microscopy70.00A/D/G/J/M/P5-844[»]
1O19electron microscopy70.00A/D/G/J/M/S5-844[»]
1O1Aelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Belectron microscopy70.00A/D/G/J5-844[»]
1O1Celectron microscopy70.00A/D/G/J/P5-844[»]
1O1Delectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Eelectron microscopy70.00A/D/G/J/M/P5-844[»]
1O1Felectron microscopy70.00A/D/G/J5-844[»]
1O1Gelectron microscopy70.00A/D/G/J/M/P5-844[»]
2MYSX-ray2.80A2-844[»]
2W4Aelectron microscopy35.00M5-844[»]
2W4Gelectron microscopy35.00M5-844[»]
2W4Helectron microscopy35.00M5-844[»]
ProteinModelPortaliP13538.
SMRiP13538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000001425.

PTM databases

iPTMnetiP13538.

Proteomic databases

PaxDbiP13538.
PRIDEiP13538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi427788.
KEGGigga:427788.

Organism-specific databases

CTDi427788.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOVERGENiHBG004704.
KOiK10352.

Miscellaneous databases

EvolutionaryTraceiP13538.
PROiP13538.

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...

Entry informationi

Entry nameiMYSS_CHICK
AccessioniPrimary (citable) accession number: P13538
Secondary accession number(s): O13228
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 149 of the entry and version 4 of the sequence. [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.