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Q3UIZ8 (MYLK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin light chain kinase 3

EC=2.7.11.18
Alternative name(s):
Cardiac-MyBP-C-associated Ca/CaM kinase
Short name=Cardiac-MLCK
Gene names
Name:Mylk3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Kinase that phosphorylates MYL2 in vitro. Has been proposed to be calmodulin-dependent (Ref.3), although MYL2 phosphorylation has also been observed in the presence or absence of calmodulin (Ref.1). Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility. Ref.1 Ref.3

Catalytic activity

ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Restricted to cardiomyocytes (at protein level). Down-regulated in heart after experimental myocardial infarction at the protein level; no significant changes at the mRNA level. Ref.1

Developmental stage

Up-regulated in the heart from 10.5 dpc to neonates and further increased in adults. Down-regulated in aged hearts (at protein level). Ref.1

Post-translational modification

Phosphorylated on serine residues. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=4.3 µM for MYL2 Ref.1

Vmax=0.26 µmol/min/mg enzyme

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UIZ8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q3UIZ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-162: Missing.
     777-795: KHFHVVTAVNRLRKFPTCP → VFWVFFSKSCI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Myosin light chain kinase 3
PRO_0000272201

Regions

Domain491 – 746256Protein kinase
Nucleotide binding497 – 5059ATP By similarity

Sites

Active site6121Proton acceptor By similarity
Binding site5201ATP By similarity

Natural variations

Alternative sequence100 – 16263Missing in isoform 2.
VSP_022369
Alternative sequence777 – 79519KHFHV…FPTCP → VFWVFFSKSCI in isoform 2.
VSP_022370

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 9B9874D50E6EBA20

FASTA79586,372
        10         20         30         40         50         60 
MSGVSEEDPE GLAPQGLPAL GGACLATMDK KLNVLTEKVD RLLHFQEDVT EKLQCVCQGM 

        70         80         90        100        110        120 
DHLEQDLHRL EASRELSLAG SGSTPPTTAQ AAWPEVLELV RAVRQEGAQH GARLEALFKM 

       130        140        150        160        170        180 
VVAVDRAITL VGSTFQNSKV ADFIMQGTVP GRKGSLADGP EENKEQAEVA GVKPNHVLTT 

       190        200        210        220        230        240 
GGVQADASRT LWEESQKEDI PVRTVEGLPL IINTSLKGAD LTQAGASLRQ GVEVLGPGQV 

       250        260        270        280        290        300 
PLPTEAESRL PETASENTGA TLELSVAIDR ISEVLTSLKM SQGGGQETSS SKPDCWLSEE 

       310        320        330        340        350        360 
AMRLSSGPLP QPLGPLTPDS DIHSGDALPR IPINMQEMAT PGELLETQSG SPIGSAEAPG 

       370        380        390        400        410        420 
LGTVLEDQIP KGARPFPPLP KRSSNNGGMS AEEEIGSGAE PMRGPSLATR DWRDETVGTT 

       430        440        450        460        470        480 
DLQQGIDPGA VSPEPGKDHA AQGPGRTEAG RLSSAAEAAI VVLDDSAAPP APFEHRVVSI 

       490        500        510        520        530        540 
KDTLISAGYT VSQHEVLGGG RFGQVHRCTE RSTGLALAAK IIKVKNVKDR EDVKNEVNIM 

       550        560        570        580        590        600 
NQLSHVNLIQ LYDAFESKSS FTLIMEYVDG GELFDRITDE KYHLTELDVV LFTRQICEGV 

       610        620        630        640        650        660 
HYLHQHYILH LDLKPENILC VSQTGHQIKI IDFGLARRYK PREKLKVNFG TPEFLAPEVV 

       670        680        690        700        710        720 
NYEFVSFPTD MWSVGVITYM LLSGLSPFLG ETDAETMNFI VNCSWDFDAD TFKGLSEEAK 

       730        740        750        760        770        780 
DFVSRLLVKE KSCRMSATQC LKHEWLSHLP AKASGSNVRL RSQQLLQKYM AQSKWKKHFH 

       790 
VVTAVNRLRK FPTCP 

« Hide

Isoform 2 [UniParc].

Checksum: AE80A5AB899A23C4
Show »

FASTA72478,790

References

« Hide 'large scale' references
[1]"Identification of cardiac-specific myosin light chain kinase."
Chan J.Y., Takeda M., Briggs L.E., Graham M.L., Lu J.T., Horikoshi N., Weinberg E.O., Aoki H., Sato N., Chien K.R., Kasahara H.
Circ. Res. 102:571-580(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Heart and Testis.
[3]"A cardiac myosin light chain kinase regulates sarcomere assembly in the vertebrate heart."
Seguchi O., Takashima S., Yamazaki S., Asakura M., Asano Y., Shintani Y., Wakeno M., Minamino T., Kondo H., Furukawa H., Nakamaru K., Naito A., Takahashi T., Ohtsuka T., Kawakami K., Isomura T., Kitamura S., Tomoike H., Mochizuki N., Kitakaze M.
J. Clin. Invest. 117:2812-2824(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU403565 mRNA. Translation: ABY89726.1.
AK031546 mRNA. Translation: BAE43277.1.
AK052858 mRNA. Translation: BAC35177.1.
AK146683 mRNA. Translation: BAE27357.1.
CCDSCCDS40422.1. [Q3UIZ8-1]
RefSeqNP_780650.2. NM_175441.5. [Q3UIZ8-1]
UniGeneMm.32804.

3D structure databases

ProteinModelPortalQ3UIZ8.
SMRQ3UIZ8. Positions 429-765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3UIZ8. 1 interaction.
MINTMINT-4112993.

PTM databases

PhosphoSiteQ3UIZ8.

Proteomic databases

MaxQBQ3UIZ8.
PaxDbQ3UIZ8.
PRIDEQ3UIZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034133; ENSMUSP00000034133; ENSMUSG00000031698. [Q3UIZ8-1]
ENSMUST00000121972; ENSMUSP00000113960; ENSMUSG00000031698. [Q3UIZ8-2]
GeneID213435.
KEGGmmu:213435.
UCSCuc009mps.1. mouse. [Q3UIZ8-1]

Organism-specific databases

CTD91807.
MGIMGI:2443063. Mylk3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117629.
HOGENOMHOG000233016.
HOVERGENHBG080416.
InParanoidQ3UIZ8.
KOK00907.
OMAFRMVVAV.
OrthoDBEOG73FQMV.
PhylomeDBQ3UIZ8.
TreeFamTF314166.

Gene expression databases

ArrayExpressQ3UIZ8.
BgeeQ3UIZ8.
CleanExMM_MYLK3.
GenevestigatorQ3UIZ8.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373954.
PROQ3UIZ8.
SOURCESearch...

Entry information

Entry nameMYLK3_MOUSE
AccessionPrimary (citable) accession number: Q3UIZ8
Secondary accession number(s): B0LY41, Q3V3V0, Q8BWD1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot