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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 – 1868ATP Reviewed prediction

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: UniProtKB-SubCell
  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-13
PRO_0000123430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301N6,N6,N6-trimethyllysine Reviewed prediction

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

ArrayExpressiQ9UKX3.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 782697Myosin motor
Add
BLAST
Domaini785 – 81430IQ
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni659 – 68123Actin-binding By similarity
Add
BLAST
Regioni761 – 77515Actin-binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili843 – 19381096 Reviewed prediction
Add
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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
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

MSSDAEMAIF GEAAPYLRKP EKERIEAQNR PFDSKKACFV ADNKEMYVKG     50
MIQTRENDKV IVKTLDDRML TLNNDQVFPM NPPKFDKIED MAMMTHLHEP 100
AVLYNLKERY AAWMIYTYSG LFCVTVNPYK WLPVYKPEVV AAYRGKKRQE 150
APPHIFSISD NAYQFMLTDR DNQSILITGE SGAGKTVNTK RVIQYFATIA 200
VTGDKKKETQ PGKMQGTLED QIIQANPLLE AFGNAKTVRN DNSSRFGKFI 250
RIHFGATGKL ASADIETYLL EKSRVTFQLS SERSYHIFYQ IMSNKKPELI 300
DLLLISTNPF DFPFVSQGEV TVASIDDSEE LLATDNAIDI LGFSSEEKVG 350
IYKLTGAVMH YGNMKFKQKQ REEQAEPDGT EVADKAGYLM GLNSAEMLKG 400
LCCPRVKVGN EYVTKGQNVQ QVTNSVGALA KAVYEKMFLW MVTRINQQLD 450
TKQPRQYFIG VLDIAGFEIF DFNSLEQLCI NFTNEKLQQF FNHHMFVLEQ 500
EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC MFPKATDTSF 550
KNKLYDQHLG KSNNFQKPKP AKGKAEAHFS LVHYAGTVDY NIAGWLDKNK 600
DPLNETVVGL YQKSSLKLLS FLFSNYAGAE TGDSGGSKKG GKKKGSSFQT 650
VSAVFRENLN KLMTNLRSTH PHFVRCLIPN ETKTPGVMDH YLVMHQLRCN 700
GVLEGIRICR KGFPSRILYA DFKQRYRILN ASAIPEGQFI DSKNASEKLL 750
NSIDVDREQF RFGNTKVFFK AGLLGLLEEM RDEKLVTLMT STQAVCRGYL 800
MRVEFKKMME RRDSIFCIQY NIRSFMNVKH WPWMNLFFKI KPLLKSAEAE 850
KEMATMKEDF ERTKEELARS EARRKELEEK MVSLLQEKND LQLQVQSETE 900
NLMDAEERCE GLIKSKILLE AKVKELTERL EEEEEMNSEL VAKKRNLEDK 950
CSSLKRDIDD LELTLTKVEK EKHATENKVK NLSEEMTALE ENISKLTKEK 1000
KSLQEAHQQT LDDLQVEEDK VNGLIKINAK LEQQTDDLEG SLEQEKKLRA 1050
DLERAKRKLE GDLKMSQESI MDLENDKQQI EEKLKKKEFE LSQLQAKIDD 1100
EQVHSLQFQK KIKELQARIE ELEEEIEAEH TLRAKIEKQR SDLARELEEI 1150
SERLEEASGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKQ 1200
ADSVAELGEQ IDNLQRVKQK LEKEKSELKM EIDDMASNIE ALSKSKSNIE 1250
RTCRTVEDQF SEIKAKDEQQ TQLIHDLNMQ KARLQTQNGE LSHRVEEKES 1300
LISQLTKSKQ ALTQQLEELK RQMEEETKAK NAMAHALQSS RHDCDLLREQ 1350
YEEEQEAKAE LQRALSKANS EVAQWRTKYE TDAIQRTEEL EEAKKKLAQR 1400
LQEAEENTET ANSKCASLEK TKQRLQGEVE DLMRDLERSH TACATLDKKQ 1450
RNFDKVLAEW KQKLDESQAE LEAAQKESRS LSTELFKMRN AYEEVVDQLE 1500
TLRRENKNLQ EEISDLTEQI AETGKNLQEA EKTKKLVEQE KSDLQVALEE 1550
VEGSLEHEES KILRVQLELS QVKSELDRKV IEKDEEIEQL KRNSQRAAEA 1600
LQSVLDAEIR SRNDALRLKK KMEGDLNEME IQLGHSNRQM AETQKHLRTV 1650
QGQLKDSQLH LDDALRSNED LKEQLAIVER RNGLLLEELE EMKVALEQTE 1700
RTRRLSEQEL LDASDRVQLL HSQNTSLINT KKKLEADIAQ CQAEVENSIQ 1750
ESRNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EQTVKDLQHR 1800
LDEAEQLALK GGKKQIQKLE NRVRELENEL DVEQKRGAEA LKGAHKYERK 1850
VKEMTYQAEE DHKNILRLQD LVDKLQAKVK SYKRQAEEAE EQANTQLSRC 1900
RRVQHELEEA AERADIAESQ VNKLRAKSRD VGSQKMEE 1938
Length:1,938
Mass (Da):223,605
Last modified:February 8, 2011 - v2
Checksum:i66DD43A84F5D38DA
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1097 – 10971K → R in AAD29948. 1 Publication
Sequence conflicti1376 – 13761R → K in AAD29948. 1 Publication
Sequence conflicti1407 – 14071N → K in AAD29948. 1 Publication
Sequence conflicti1645 – 16451K → R in AAD29948. 1 Publication

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.
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 .
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.
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

ArrayExpressi Q9UKX3.
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: September 3, 2014
This is version 126 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

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