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Q9UKX3

- MYH13_HUMAN

UniProt

Q9UKX3 - MYH13_HUMAN

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Protein

Myosin-13

Gene

MYH13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Fast twitching myosin mediating the high-velocity and low-tension contractions of specific striated muscles.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1868ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microfilament motor activity Source: UniProtKB

GO - Biological processi

  1. cellular response to starvation Source: Ensembl
  2. metabolic process Source: GOC
  3. muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-13
Alternative name(s):
Myosin heavy chain 13
Myosin heavy chain, skeletal muscle, extraocular
Short name:
MyHC-EO
Myosin heavy chain, skeletal muscle, laryngeal
Short name:
MyHC-IIL
Superfast myosin
Gene namesi
Name:MYH13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7571. MYH13.

Subcellular locationi

Cytoplasmmyofibril
Note: Thick filaments of the myofibrils.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. muscle myosin complex Source: UniProtKB
  3. myofibril Source: Ensembl
  4. myosin filament Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Thick filament

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19381938Myosin-13PRO_0000123430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301N6,N6,N6-trimethyllysineSequence Analysis

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiQ9UKX3.
PaxDbiQ9UKX3.
PeptideAtlasiQ9UKX3.
PRIDEiQ9UKX3.

PTM databases

PhosphoSiteiQ9UKX3.

Expressioni

Tissue specificityi

Specifically expressed in extraocular and laryngeal muscles.1 Publication

Gene expression databases

BgeeiQ9UKX3.
CleanExiHS_MYH13.
GenevestigatoriQ9UKX3.

Organism-specific databases

HPAiCAB000140.

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

BioGridi114272. 2 interactions.
IntActiQ9UKX3. 3 interactions.
MINTiMINT-2821927.
STRINGi9606.ENSP00000252172.

Structurei

3D structure databases

ProteinModelPortaliQ9UKX3.
SMRiQ9UKX3. Positions 4-965.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 782697Myosin motorAdd
BLAST
Domaini785 – 81430IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni659 – 68123Actin-bindingBy similarityAdd
BLAST
Regioni761 – 77515Actin-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili843 – 19381096Sequence 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).
The head-like domain S1 exhibits a much faster ATP-induced detachment from actin, and ADP affinity is more than 3-fold weaker than other myosins.

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118919.
HOGENOMiHOG000173959.
HOVERGENiHBG004704.
InParanoidiQ9UKX3.
KOiK10352.
OMAiGCLEQEK.
OrthoDBiEOG7RBZ7G.
PhylomeDBiQ9UKX3.
TreeFamiTF314375.

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.

Q9UKX3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSDAEMAIF GEAAPYLRKP EKERIEAQNR PFDSKKACFV ADNKEMYVKG
60 70 80 90 100
MIQTRENDKV IVKTLDDRML TLNNDQVFPM NPPKFDKIED MAMMTHLHEP
110 120 130 140 150
AVLYNLKERY AAWMIYTYSG LFCVTVNPYK WLPVYKPEVV AAYRGKKRQE
160 170 180 190 200
APPHIFSISD NAYQFMLTDR DNQSILITGE SGAGKTVNTK RVIQYFATIA
210 220 230 240 250
VTGDKKKETQ PGKMQGTLED QIIQANPLLE AFGNAKTVRN DNSSRFGKFI
260 270 280 290 300
RIHFGATGKL ASADIETYLL EKSRVTFQLS SERSYHIFYQ IMSNKKPELI
310 320 330 340 350
DLLLISTNPF DFPFVSQGEV TVASIDDSEE LLATDNAIDI LGFSSEEKVG
360 370 380 390 400
IYKLTGAVMH YGNMKFKQKQ REEQAEPDGT EVADKAGYLM GLNSAEMLKG
410 420 430 440 450
LCCPRVKVGN EYVTKGQNVQ QVTNSVGALA KAVYEKMFLW MVTRINQQLD
460 470 480 490 500
TKQPRQYFIG VLDIAGFEIF DFNSLEQLCI NFTNEKLQQF FNHHMFVLEQ
510 520 530 540 550
EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC MFPKATDTSF
560 570 580 590 600
KNKLYDQHLG KSNNFQKPKP AKGKAEAHFS LVHYAGTVDY NIAGWLDKNK
610 620 630 640 650
DPLNETVVGL YQKSSLKLLS FLFSNYAGAE TGDSGGSKKG GKKKGSSFQT
660 670 680 690 700
VSAVFRENLN KLMTNLRSTH PHFVRCLIPN ETKTPGVMDH YLVMHQLRCN
710 720 730 740 750
GVLEGIRICR KGFPSRILYA DFKQRYRILN ASAIPEGQFI DSKNASEKLL
760 770 780 790 800
NSIDVDREQF RFGNTKVFFK AGLLGLLEEM RDEKLVTLMT STQAVCRGYL
810 820 830 840 850
MRVEFKKMME RRDSIFCIQY NIRSFMNVKH WPWMNLFFKI KPLLKSAEAE
860 870 880 890 900
KEMATMKEDF ERTKEELARS EARRKELEEK MVSLLQEKND LQLQVQSETE
910 920 930 940 950
NLMDAEERCE GLIKSKILLE AKVKELTERL EEEEEMNSEL VAKKRNLEDK
960 970 980 990 1000
CSSLKRDIDD LELTLTKVEK EKHATENKVK NLSEEMTALE ENISKLTKEK
1010 1020 1030 1040 1050
KSLQEAHQQT LDDLQVEEDK VNGLIKINAK LEQQTDDLEG SLEQEKKLRA
1060 1070 1080 1090 1100
DLERAKRKLE GDLKMSQESI MDLENDKQQI EEKLKKKEFE LSQLQAKIDD
1110 1120 1130 1140 1150
EQVHSLQFQK KIKELQARIE ELEEEIEAEH TLRAKIEKQR SDLARELEEI
1160 1170 1180 1190 1200
SERLEEASGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKQ
1210 1220 1230 1240 1250
ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDMASNIE ALSKSKSNIE
1260 1270 1280 1290 1300
RTCRTVEDQF SEIKAKDEQQ TQLIHDLNMQ KARLQTQNGE LSHRVEEKES
1310 1320 1330 1340 1350
LISQLTKSKQ ALTQQLEELK RQMEEETKAK NAMAHALQSS RHDCDLLREQ
1360 1370 1380 1390 1400
YEEEQEAKAE LQRALSKANS EVAQWRTKYE TDAIQRTEEL EEAKKKLAQR
1410 1420 1430 1440 1450
LQEAEENTET ANSKCASLEK TKQRLQGEVE DLMRDLERSH TACATLDKKQ
1460 1470 1480 1490 1500
RNFDKVLAEW KQKLDESQAE LEAAQKESRS LSTELFKMRN AYEEVVDQLE
1510 1520 1530 1540 1550
TLRRENKNLQ EEISDLTEQI AETGKNLQEA EKTKKLVEQE KSDLQVALEE
1560 1570 1580 1590 1600
VEGSLEHEES KILRVQLELS QVKSELDRKV IEKDEEIEQL KRNSQRAAEA
1610 1620 1630 1640 1650
LQSVLDAEIR SRNDALRLKK KMEGDLNEME IQLGHSNRQM AETQKHLRTV
1660 1670 1680 1690 1700
QGQLKDSQLH LDDALRSNED LKEQLAIVER RNGLLLEELE EMKVALEQTE
1710 1720 1730 1740 1750
RTRRLSEQEL LDASDRVQLL HSQNTSLINT KKKLEADIAQ CQAEVENSIQ
1760 1770 1780 1790 1800
ESRNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EQTVKDLQHR
1810 1820 1830 1840 1850
LDEAEQLALK GGKKQIQKLE NRVRELENEL DVEQKRGAEA LKGAHKYERK
1860 1870 1880 1890 1900
VKEMTYQAEE DHKNILRLQD LVDKLQAKVK SYKRQAEEAE EQANTQLSRC
1910 1920 1930
RRVQHELEEA AERADIAESQ VNKLRAKSRD VGSQKMEE
Length:1,938
Mass (Da):223,605
Last modified:February 8, 2011 - v2
Checksum:i66DD43A84F5D38DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1097 – 10971K → R in AAD29948. (PubMed:10388558)Curated
Sequence conflicti1376 – 13761R → K in AAD29948. (PubMed:10388558)Curated
Sequence conflicti1407 – 14071N → K in AAD29948. (PubMed:10388558)Curated
Sequence conflicti1645 – 16451K → R in AAD29948. (PubMed:10388558)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti701 – 7011G → R.
Corresponds to variant rs2190729 [ dbSNP | Ensembl ].
VAR_030231
Natural varianti1071 – 10711M → V.
Corresponds to variant rs2074877 [ dbSNP | Ensembl ].
VAR_024543
Natural varianti1076 – 10761D → E.1 Publication
Corresponds to variant rs2074876 [ dbSNP | Ensembl ].
VAR_030232
Natural varianti1294 – 12941R → Q.
Corresponds to variant rs17690195 [ dbSNP | Ensembl ].
VAR_030233
Natural varianti1862 – 18621H → R.1 Publication
Corresponds to variant rs3744550 [ dbSNP | Ensembl ].
VAR_030234

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF111782 mRNA. Translation: AAD29948.1.
AC005291 Genomic DNA. No translation available.
AH009397 Genomic DNA. Translation: AAF73155.1.
AF075248 Genomic DNA. Translation: AAC83241.1.
CCDSiCCDS45613.1.
RefSeqiNP_003793.2. NM_003802.2.
UniGeneiHs.711142.

Genome annotation databases

EnsembliENST00000252172; ENSP00000252172; ENSG00000006788.
ENST00000418404; ENSP00000404570; ENSG00000006788.
ENST00000621918; ENSP00000480864; ENSG00000006788.
GeneIDi8735.
KEGGihsa:8735.
UCSCiuc002gmk.1. human.

Polymorphism databases

DMDMi322510049.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF111782 mRNA. Translation: AAD29948.1 .
AC005291 Genomic DNA. No translation available.
AH009397 Genomic DNA. Translation: AAF73155.1 .
AF075248 Genomic DNA. Translation: AAC83241.1 .
CCDSi CCDS45613.1.
RefSeqi NP_003793.2. NM_003802.2.
UniGenei Hs.711142.

3D structure databases

ProteinModelPortali Q9UKX3.
SMRi Q9UKX3. Positions 4-965.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114272. 2 interactions.
IntActi Q9UKX3. 3 interactions.
MINTi MINT-2821927.
STRINGi 9606.ENSP00000252172.

PTM databases

PhosphoSitei Q9UKX3.

Polymorphism databases

DMDMi 322510049.

Proteomic databases

MaxQBi Q9UKX3.
PaxDbi Q9UKX3.
PeptideAtlasi Q9UKX3.
PRIDEi Q9UKX3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252172 ; ENSP00000252172 ; ENSG00000006788 .
ENST00000418404 ; ENSP00000404570 ; ENSG00000006788 .
ENST00000621918 ; ENSP00000480864 ; ENSG00000006788 .
GeneIDi 8735.
KEGGi hsa:8735.
UCSCi uc002gmk.1. human.

Organism-specific databases

CTDi 8735.
GeneCardsi GC17M010201.
H-InvDB HIX0039060.
HGNCi HGNC:7571. MYH13.
HPAi CAB000140.
MIMi 603487. gene.
neXtProti NX_Q9UKX3.
PharmGKBi PA31368.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00760000118919.
HOGENOMi HOG000173959.
HOVERGENi HBG004704.
InParanoidi Q9UKX3.
KOi K10352.
OMAi GCLEQEK.
OrthoDBi EOG7RBZ7G.
PhylomeDBi Q9UKX3.
TreeFami TF314375.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSi MYH13. human.
GeneWikii MYH13.
GenomeRNAii 8735.
NextBioi 32765.
PROi Q9UKX3.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKX3.
CleanExi HS_MYH13.
Genevestigatori Q9UKX3.

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

« Hide 'large scale' publications
  1. "Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity."
    Weiss A., Schiaffino S., Leinwand L.A.
    J. Mol. Biol. 290:61-75(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLU-1076 AND ARG-1862.
    Tissue: Extraocular muscle.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human skeletal myosin heavy chain genes are tightly linked in the order embryonic-IIa-IId/x-ILb-perinatal-extraocular."
    Shrager J.B., Desjardins P.R., Burkman J.M., Konig S.K., Stewart S.K., Su L., Shah M.C., Bricklin E., Tewari M., Hoffman R., Rickels M.R., Jullian E.H., Rubinstein N.A., Stedman H.H.
    J. Muscle Res. Cell Motil. 21:345-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1656-1822.
  4. "The human extraocular muscle myosin heavy chain gene (MYH13) maps to the cluster of fast and developmental myosin genes on chromosome 17."
    Winters L.M., Briggs M.M., Schachat F.
    Genomics 54:188-189(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1917-1938.
    Tissue: Extraocular muscle.
  5. "Phylogenetic implications of the superfast myosin in extraocular muscles."
    Schachat F., Briggs M.M.
    J. Exp. Biol. 205:2189-2201(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "The superfast human extraocular myosin is kinetically distinct from the fast skeletal IIa, IIb, and IId isoforms."
    Bloemink M.J., Deacon J.C., Resnicow D.I., Leinwand L.A., Geeves M.A.
    J. Biol. Chem. 288:27469-27479(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMYH13_HUMAN
AccessioniPrimary (citable) accession number: Q9UKX3
Secondary accession number(s): O95252, Q9P0U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 8, 2011
Last modified: October 29, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3