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Protein

Myosin heavy chain, skeletal muscle, adult

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

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

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, 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).

GO - Molecular functioni

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
Beta strandi40 – 42Combined sources3
Beta strandi44 – 49Combined sources6
Beta strandi51 – 55Combined sources5
Beta strandi62 – 65Combined sources4
Helixi75 – 77Combined sources3
Helixi92 – 94Combined sources3
Helixi100 – 107Combined sources8
Turni111 – 114Combined sources4
Beta strandi117 – 119Combined sources3
Beta strandi124 – 127Combined sources4
Helixi134 – 136Combined sources3
Turni141 – 146Combined sources6
Helixi156 – 170Combined sources15
Beta strandi174 – 180Combined sources7
Helixi186 – 190Combined sources5
Helixi193 – 200Combined sources8
Helixi219 – 234Combined sources16
Beta strandi242 – 245Combined sources4
Beta strandi247 – 255Combined sources9
Beta strandi257 – 263Combined sources7
Turni275 – 277Combined sources3
Helixi287 – 292Combined sources6
Helixi299 – 304Combined sources6
Helixi310 – 312Combined sources3
Helixi314 – 316Combined sources3
Helixi328 – 341Combined sources14
Turni346 – 348Combined sources3
Turni351 – 353Combined sources3
Helixi358 – 362Combined sources5
Beta strandi367 – 370Combined sources4
Beta strandi375 – 379Combined sources5
Turni383 – 385Combined sources3
Helixi388 – 391Combined sources4
Helixi395 – 403Combined sources9
Beta strandi410 – 412Combined sources3
Helixi420 – 431Combined sources12
Turni434 – 436Combined sources3
Helixi439 – 449Combined sources11
Beta strandi458 – 466Combined sources9
Beta strandi472 – 474Combined sources3
Helixi476 – 486Combined sources11
Helixi489 – 503Combined sources15
Helixi518 – 528Combined sources11
Helixi533 – 540Combined sources8
Helixi548 – 551Combined sources4
Helixi556 – 559Combined sources4
Beta strandi563 – 567Combined sources5
Beta strandi579 – 583Combined sources5
Beta strandi588 – 591Combined sources4
Turni596 – 598Combined sources3
Helixi606 – 613Combined sources8
Helixi620 – 623Combined sources4
Helixi651 – 659Combined sources9
Helixi662 – 666Combined sources5
Beta strandi668 – 676Combined sources9
Helixi689 – 699Combined sources11
Helixi701 – 708Combined sources8
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 – 782Combined sources11
Helixi785 – 827Combined sources43
Turni831 – 833Combined 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
Domaini34 – 83Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST50
Domaini87 – 781Myosin motorPROSITE-ProRule annotationAdd 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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161 Eukaryota
COG5022 LUCA
HOVERGENiHBG004704
KOiK10352

Family and domain databases

Gene3Di2.30.30.360, 1 hit
3.40.850.10, 3 hits
4.10.270.10, 1 hit
InterProiView protein in InterPro
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR027401 Myosin_IQ_contain_sf
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.

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

Similar proteinsi

Entry informationi

Entry nameiMYSS_CHICK
AccessioniPrimary (citable) accession number: P13538
Secondary accession number(s): O13228
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 156 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

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