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P13538

- MYSS_CHICK

UniProt

P13538 - MYSS_CHICK

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Protein

Myosin heavy chain, skeletal muscle, adult

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1878ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. motor activity Source: InterPro
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Cytoplasmmyofibril
Note: Thick filaments of the myofibrils.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. myosin filament Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 19391938Myosin heavy chain, skeletal muscle, adultPRO_0000123434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei36 – 361N6-methyllysine1 Publication
Modified residuei131 – 1311N6,N6,N6-trimethyllysine1 Publication
Modified residuei552 – 5521N6,N6,N6-trimethyllysine1 Publication
Modified residuei756 – 7561Pros-methylhistidine1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP13538.
PRIDEiP13538.

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).

Structurei

Secondary structure

1
1939
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 184Combined sources
Turni22 – 254Combined sources
Helixi26 – 294Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 425Combined sources
Beta strandi44 – 5613Combined sources
Beta strandi58 – 636Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 744Combined sources
Helixi75 – 773Combined sources
Beta strandi86 – 883Combined sources
Helixi92 – 943Combined sources
Helixi100 – 10910Combined sources
Turni110 – 1145Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi124 – 1274Combined sources
Helixi134 – 1363Combined sources
Helixi140 – 1434Combined sources
Turni144 – 1463Combined sources
Helixi156 – 17015Combined sources
Beta strandi174 – 1807Combined sources
Helixi186 – 20015Combined sources
Helixi219 – 23416Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi247 – 2559Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi266 – 2694Combined sources
Helixi273 – 2764Combined sources
Helixi287 – 2926Combined sources
Helixi298 – 3047Combined sources
Helixi310 – 3123Combined sources
Helixi314 – 3163Combined sources
Helixi328 – 34114Combined sources
Helixi346 – 36217Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi376 – 3794Combined sources
Helixi383 – 3919Combined sources
Helixi395 – 4039Combined sources
Beta strandi410 – 4123Combined sources
Helixi420 – 44930Combined sources
Beta strandi458 – 4669Combined sources
Beta strandi472 – 4743Combined sources
Helixi476 – 50631Combined sources
Helixi518 – 52811Combined sources
Helixi533 – 5408Combined sources
Helixi548 – 55912Combined sources
Beta strandi563 – 5675Combined sources
Beta strandi579 – 5835Combined sources
Beta strandi588 – 5914Combined sources
Helixi596 – 6016Combined sources
Helixi606 – 6138Combined sources
Helixi618 – 6236Combined sources
Helixi651 – 66616Combined sources
Beta strandi668 – 6769Combined sources
Helixi689 – 69911Combined sources
Helixi701 – 7088Combined sources
Beta strandi715 – 7173Combined sources
Helixi718 – 7258Combined sources
Helixi726 – 7283Combined sources
Turni729 – 7313Combined sources
Helixi743 – 7486Combined sources
Beta strandi751 – 7533Combined sources
Beta strandi756 – 7627Combined sources
Beta strandi765 – 7684Combined sources
Helixi772 – 82756Combined sources
Helixi831 – 8399Combined sources
Turni840 – 8423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 841-966.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13538.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 781695Myosin motorAdd
BLAST
Domaini784 – 81330IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni658 – 68023Actin-bindingAdd
BLAST
Regioni760 – 77415Actin-bindingAdd
BLAST
Regioni839 – 8413Hinge

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili842 – 19391098Sequence 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.
Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti908 – 9081C → Q AA sequence (PubMed:2610940)Curated
Sequence conflicti908 – 9081C → Q AA sequence (PubMed:2775482)Curated
Sequence conflicti981 – 9811L → F in AAB47555. (PubMed:9358064)Curated
Sequence conflicti1344 – 13441E → D AA sequence (PubMed:1939030)Curated
Sequence conflicti1546 – 15461S → A AA sequence (PubMed:1939030)Curated
Sequence conflicti1797 – 17982HV → QL AA sequence (PubMed:1939030)Curated
Sequence conflicti1831 – 18311S → A AA sequence (PubMed:1939030)Curated
Sequence conflicti1864 – 18641I → V in AAA48970. (PubMed:3034534)Curated
Sequence conflicti1930 – 19323IHG → FH in AAA48970. (PubMed:3034534)Curated

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.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 .
RefSeqi NP_001013415.1. NM_001013397.2.
UniGenei Gga.51379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ALM model - A 1-844 [» ]
1M8Q electron microscopy 70.00 A/D/G/P 5-844 [» ]
1MVW electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
1O18 electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
1O19 electron microscopy 70.00 A/D/G/J/M/S 5-844 [» ]
1O1A electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
1O1B electron microscopy 70.00 A/D/G/J 5-844 [» ]
1O1C electron microscopy 70.00 A/D/G/J/P 5-844 [» ]
1O1D electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
1O1E electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
1O1F electron microscopy 70.00 A/D/G/J 5-844 [» ]
1O1G electron microscopy 70.00 A/D/G/J/M/P 5-844 [» ]
2MYS X-ray 2.80 A 2-844 [» ]
2W4A electron microscopy 35.00 M 5-844 [» ]
2W4G electron microscopy 35.00 M 5-844 [» ]
2W4H electron microscopy 35.00 M 5-844 [» ]
ProteinModelPortali P13538.
SMRi P13538. Positions 841-966.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P13538.
PRIDEi P13538.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 427788.
KEGGi gga:427788.

Organism-specific databases

CTDi 427788.

Phylogenomic databases

eggNOGi COG5022.
HOVERGENi HBG004704.
KOi K10352.

Miscellaneous databases

EvolutionaryTracei P13538.
NextBioi 20828954.

Family and domain databases

Gene3Di 4.10.270.10. 1 hit.
InterProi IPR000048. 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 ]
Pfami PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view ]
PRINTSi PR00193. MYOSINHEAVY.
SMARTi SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, nucleotide sequence and characterization of a full-length cDNA encoding the myosin heavy chain from adult chicken pectoralis major muscle."
    Chao T.H., Bandman E.
    Gene 199:265-270(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: White leghorn.
    Tissue: Pectoralis muscle.
  2. "The primary structure of skeletal muscle myosin heavy chain: I. Sequence of the amino-terminal 23 kDa fragment."
    Hayashida M., Maita T., Matsuda G.
    J. Biochem. 110:54-59(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-206.
    Tissue: Pectoralis muscle.
  3. "The primary structure of skeletal muscle myosin heavy chain: II. Sequence of the 50 kDa fragment of subfragment-1."
    Komine Y., Maita T., Matsuda G.
    J. Biochem. 110:60-67(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 207-637.
    Tissue: Pectoralis muscle.
  4. "The primary structure of skeletal muscle myosin heavy chain: III. Sequence of the 22 kDa fragment and the alignment of the 23 kDa, 50 kDa, and 22 kDa fragments."
    Maita T., Miyanishi T., Matsuzono K., Tanioka Y., Matsuda G.
    J. Biochem. 110:68-74(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 638-838.
    Tissue: Pectoralis muscle.
  5. "The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain."
    Maita T., Yajima E., Nagata S., Miyanishi T., Nakayama S., Matsuda G.
    J. Biochem. 110:75-87(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 839-1939.
    Tissue: Pectoralis muscle.
  6. Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-809, ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT LYS-36; LYS-131; LYS-552 AND HIS-756.
  7. "Complete amino-acid sequence of subfragment-2 in adult chicken skeletal muscle myosin."
    Watanabe B.
    Biol. Chem. Hoppe-Seyler 370:1027-1034(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 843-1271.
  8. "Amino-acid sequence of the short subfragment-2 in adult chicken skeletal muscle myosin."
    Watanabe B.
    Biol. Chem. Hoppe-Seyler 370:549-558(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 853-1109.
  9. "Amino-acid sequence of the hinge region in chicken myosin subfragment-2."
    Watanabe B.
    Biol. Chem. Hoppe-Seyler 370:55-61(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1146-1271.
  10. "Genomic clones encoding chicken myosin heavy-chain genes."
    Moriarity D.M., Barringer K.J., Dodgson J.B., Richter H.E., Young R.B.
    DNA 6:91-99(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1858-1939.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-844.

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 26, 2014
This is version 136 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

External Data

Dasty 3