Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myosin light chain kinase 3

Gene

Mylk3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calmodulin-dependent kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes. Increases cardiomyocyte contractility.2 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei511 – 5111ATPPROSITE-ProRule annotation
Active sitei603 – 6031Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi488 – 4969ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: BHF-UCL
  • myosin light chain kinase activity Source: BHF-UCL

GO - Biological processi

  • cardiac myofibril assembly Source: BHF-UCL
  • cellular response to interleukin-1 Source: Ensembl
  • positive regulation of sarcomere organization Source: BHF-UCL
  • protein phosphorylation Source: BHF-UCL
  • regulation of vascular permeability involved in acute inflammatory response Source: Ensembl
  • sarcomere organization Source: BHF-UCL
  • sarcomerogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Mylk3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1305801. Mylk3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • cytosol Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786Myosin light chain kinase 3PRO_0000419665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphoserineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiE9PT87.

PTM databases

iPTMnetiE9PT87.

Expressioni

Tissue specificityi

Expressed in cardiomyocytes (at protein level). Up-regulated in heart after experimental myocardial infarction at the mRNA level.2 Publications

Developmental stagei

Up-regulated in the heart from 1 week after birth through adulthood.1 Publication

Inductioni

by NRG1 (at protein level).1 Publication

Gene expression databases

GenevisibleiE9PT87. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023657.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini482 – 737256Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
InParanoidiE9PT87.
KOiK00907.
OMAiKPKHALS.
OrthoDBiEOG73FQMV.
TreeFamiTF314166.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PT87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGVSEEDPE GLGPQGLPAL GGACLVTVDK KLNVLTEKVD RLLHFQEDVT
60 70 80 90 100
EKLQCVCQGM DHLEQGLHRL EASQELGLAG PGSTSPAAAQ AAWPEVLELV
110 120 130 140 150
RAVRQEGAQH GARLEALFKM VVAVDRAITL VGSTIQNSKV DDFILQGTVP
160 170 180 190 200
WRKGSLADGP EENKEQAEVA GVKPKHVLNT GSVQAATSRA LWEESQKQDT
210 220 230 240 250
PVGTVEGLPL IIDTSLKGAD LTQAGASLRQ GVEALDPGQE PPPTEAESRL
260 270 280 290 300
PALASEDTGT TLELSVAIDR ISEVLTSLRM SQSAGEGTSS SKPDCSEPGP
310 320 330 340 350
QPLGPLTTDS DIHSDEGLPR ISVRMREMTT PEELFETQGG SPIGSAEAPG
360 370 380 390 400
PGTVLEDQIP KGARPFPPLP KRSCNNGGAS AEEATGPGAE PIRGPSLVTR
410 420 430 440 450
DWRDEPVGTT DLQQGRDPGA VSPEPGKDHA AQGPGRTEAG RRVSSAAEAA
460 470 480 490 500
IVVLDDSAAP PAPFEHRVVS IKDTLISTSY TVSQHEVLGG GRFGQVHRCT
510 520 530 540 550
ERSTGLALAA KIIKVKNIKD REDVKNEINI MNQLSHVNLI QLYDAFESKN
560 570 580 590 600
SFTLIMEYVD GGELFDRITD EKYHLTELDV VLFTRQICEG VHYLHQHYIL
610 620 630 640 650
HLDLKPENIL CVSQTGHQIK IIDFGLARRY KPREKLKVNF GTPEFLAPEV
660 670 680 690 700
VNYEFVSFPT DMWSVGVITY MLLSGLSPFL GETDAETMNF IVNCSWDFDA
710 720 730 740 750
DTFKGLSEEA KDFVSRLLVK EKSCRMSATQ CLKHEWLNHL IAKASGSNVR
760 770 780
LRSQLLLQKY MAQRKWKKHF HVVTAVNRLR KFPTCP
Length:786
Mass (Da):85,541
Last modified:April 5, 2011 - v1
Checksum:i3355DA69E4FCBB26
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441T → A in ABW96144 (PubMed:20615916).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU236721 mRNA. Translation: ABW96144.1.
RefSeqiNP_001104280.1. NM_001110810.1.
UniGeneiRn.204358.

Genome annotation databases

EnsembliENSRNOT00000023657; ENSRNOP00000023657; ENSRNOG00000017546.
GeneIDi291926.
KEGGirno:291926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU236721 mRNA. Translation: ABW96144.1.
RefSeqiNP_001104280.1. NM_001110810.1.
UniGeneiRn.204358.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023657.

PTM databases

iPTMnetiE9PT87.

Proteomic databases

PaxDbiE9PT87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023657; ENSRNOP00000023657; ENSRNOG00000017546.
GeneIDi291926.
KEGGirno:291926.

Organism-specific databases

CTDi91807.
RGDi1305801. Mylk3.

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
InParanoidiE9PT87.
KOiK00907.
OMAiKPKHALS.
OrthoDBiEOG73FQMV.
TreeFamiTF314166.

Miscellaneous databases

PROiE9PT87.

Gene expression databases

GenevisibleiE9PT87. RN.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cardiac functional improvement in rats with myocardial infarction by up-regulating cardiac myosin light chain kinase with neuregulin."
    Gu X., Liu X., Xu D., Li X., Yan M., Qi Y., Yan W., Wang W., Pan J., Xu Y., Xi B., Cheng L., Jia J., Wang K., Ge J., Zhou M.
    Cardiovasc. Res. 88:334-343(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    Strain: Wistar.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-341 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMYLK3_RAT
AccessioniPrimary (citable) accession number: E9PT87
Secondary accession number(s): A8WE96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: April 5, 2011
Last modified: June 8, 2016
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.