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Q8VCR8 (MYLK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin light chain kinase 2, skeletal/cardiac muscle

Short name=MLCK2
EC=2.7.11.18
Gene names
Name:Mylk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain By similarity.

Catalytic activity

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

Subunit structure

May interact with centrin By similarity.

Subcellular location

Cytoplasm By similarity. Note: Colocalizes with phosphorylated myosin light chain (RLCP) at filaments of the myofibrils By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Non-traceable author statement PubMed 21556048. Source: UniProtKB

cardiac muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 16606832. Source: MGI

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of muscle filament sliding

Inferred from electronic annotation. Source: Ensembl

satellite cell differentiation

Inferred from mutant phenotype PubMed 21556048. Source: UniProtKB

skeletal muscle cell differentiation

Non-traceable author statement PubMed 21556048. Source: UniProtKB

striated muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin light chain kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 613612Myosin light chain kinase 2, skeletal/cardiac muscle
PRO_0000086409

Regions

Domain302 – 557256Protein kinase
Nucleotide binding308 – 3169ATP By similarity
Region591 – 60313Calmodulin-binding By similarity
Compositional bias96 – 1038Poly-Gly
Compositional bias278 – 2858Poly-Pro

Sites

Active site4231Proton acceptor By similarity
Binding site3311ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VCR8 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 1FAC64C8B09DAE25

FASTA61365,990
        10         20         30         40         50         60 
MTTENGAVEL GSQSLSTEQT PKAAAGDGPS ASEKEPSAPA TEKDLSPPNA KKDPGAPDPK 

        70         80         90        100        110        120 
NNPDPPSLKK DPAKAPGPEK KGDPVPASAS SQGPSGEGDG GGGPAEGSEG PPAALPLPTA 

       130        140        150        160        170        180 
TAEASIQKLD PTQAPSGNQG SGEAKAGKKA AECREAGRRG SPAFLHSPSC PAIISCSEKT 

       190        200        210        220        230        240 
LAVKPLSETT DLVFTGVSVT PDPQDPGPVK AGGTNALAEK KKEEAEKASG QAGQAKVQGD 

       250        260        270        280        290        300 
TPQRIGFQAV PSERVEVGQA LCLTAREEDC FQILDDCPPP PAPFPHRIVE LRTGNVNSEF 

       310        320        330        340        350        360 
SMNSKEALGG GKFGAVCTCT ERATGLKLAA KVIKKQTPKD KEMVLLEIEV MNQLNHRNLI 

       370        380        390        400        410        420 
QLYAAIETSH EIILFMEYIE GGELFERIVD EDYHLTEVDT MVFVRQICDG ILFMHKMRVL 

       430        440        450        460        470        480 
HLDLKPENIL CVNTTGHLVK IIDFGLARRY NPNEKLKVNF GTPEFLSPEV VNYDQISDKT 

       490        500        510        520        530        540 
DMWSLGVITY MLLSGLSPFL GDDDTETLNN VLSANWYFDE ETFEAVSDEA KDFVSNLLTK 

       550        560        570        580        590        600 
DQSARMSAEQ CLAHPWLNNL AEKAKRCNRR LKSQILLKKY LMKRRWKKNF IAVSAANRFK 

       610 
KISSSGALMA LGV 

« Hide

References

[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] OF 1-591.
Strain: C57BL/6J.
Tissue: Bone.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-613.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL833801 Genomic DNA. Translation: CAM23678.1.
AK079396 mRNA. No translation available.
BC019408 mRNA. Translation: AAH19408.1.
RefSeqNP_001074513.2. NM_001081044.2.
UniGeneMm.250604.

3D structure databases

ProteinModelPortalQ8VCR8.
SMRQ8VCR8. Positions 217-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VCR8. 2 interactions.

PTM databases

PhosphoSiteQ8VCR8.

Proteomic databases

PaxDbQ8VCR8.
PRIDEQ8VCR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028970; ENSMUSP00000028970; ENSMUSG00000027470.
GeneID228785.
KEGGmmu:228785.
UCSCuc008ngs.2. mouse.

Organism-specific databases

CTD85366.
MGIMGI:2139434. Mylk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117629.
HOGENOMHOG000233016.
HOVERGENHBG080416.
KOK00907.
OMACFQILXG.
OrthoDBEOG73FQMV.
TreeFamTF314166.

Gene expression databases

BgeeQ8VCR8.
GenevestigatorQ8VCR8.

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

ChiTaRSMYLK2. mouse.
NextBio379136.
PROQ8VCR8.
SOURCESearch...

Entry information

Entry nameMYLK2_MOUSE
AccessionPrimary (citable) accession number: Q8VCR8
Secondary accession number(s): A2APB9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 106 of the entry and version 2 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