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Q32MK0 (MYLK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
Synonyms:MLCK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length819 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility By similarity.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Restricted to heart. Ref.6

Post-translational modification

Phosphorylated on serine residues By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAI09098.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC42766.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac myofibril assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to interleukin-1

Inferred from mutant phenotype PubMed 18390750. Source: BHF-UCL

positive regulation of sarcomere organization

Inferred from sequence or structural similarity. Source: BHF-UCL

protein phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of vascular permeability involved in acute inflammatory response

Inferred from mutant phenotype PubMed 18390750. Source: BHF-UCL

sarcomere organization

Inferred from sequence or structural similarity. Source: BHF-UCL

sarcomerogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

myosin light chain kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q32MK0-3)

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: Q32MK0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-341: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 819819Myosin light chain kinase 3
PRO_0000272200

Regions

Domain515 – 770256Protein kinase
Nucleotide binding521 – 5299ATP By similarity

Sites

Active site6361Proton acceptor By similarity
Binding site5441ATP By similarity

Natural variations

Alternative sequence1 – 341341Missing in isoform 2.
VSP_044312
Natural variant701S → T.
Corresponds to variant rs9923813 [ dbSNP | Ensembl ].
VAR_058335
Natural variant1801V → L. Ref.1 Ref.5
Corresponds to variant rs28407821 [ dbSNP | Ensembl ].
VAR_058336
Natural variant3901G → R in a colorectal cancer sample; somatic mutation. Ref.7
VAR_035630

Experimental info

Sequence conflict1491R → G in BAG70269. Ref.2
Sequence conflict1991G → R in CAC42766. Ref.1

Sequences

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

Last modified July 28, 2009. Version 3.
Checksum: 21148BBACB0FF0D9

FASTA81988,393
        10         20         30         40         50         60 
MSGTSKESLG HGGLPGLGKT CLTTMDTKLN MLNEKVDQLL HFQEDVTEKL QSMCRDMGHL 

        70         80         90        100        110        120 
ERGLHRLEAS RAPGPGGADG VPHIDTQAGW PEVLELVRAM QQDAAQHGAR LEALFRMVAA 

       130        140        150        160        170        180 
VDRAIALVGA TFQKSKVADF LMQGRVPWRR GSPGDSPEEN KERVEEEGGK PKHVLSTSGV 

       190        200        210        220        230        240 
QSDAREPGEE SQKADVLEGT AERLPPIRAS GLGADPAQAV VSPGQGDGVP GPAQAFPGHL 

       250        260        270        280        290        300 
PLPTKVEAKA PETPSENLRT GLELAPAPGR VNVVSPSLEV APGAGQGASS SRPDPEPLEE 

       310        320        330        340        350        360 
GTRLTPGPGP QCPGPPGLPA QARATHSGGE TPPRISIHIQ EMDTPGEMLM TGRGSLGPTL 

       370        380        390        400        410        420 
TTEAPAAAQP GKQGPPGTGR CLQAPGTEPG EQTPEGAREL SPLQESSSPG GVKAEEEQRA 

       430        440        450        460        470        480 
GAEPGTRPSL ARSDDNDHEV GALGLQQGKS PGAGNPEPEQ DCAARAPVRA EAVRRMPPGA 

       490        500        510        520        530        540 
EAGSVVLDDS PAPPAPFEHR VVSVKETSIS AGYEVCQHEV LGGGRFGQVH RCTEKSTGLP 

       550        560        570        580        590        600 
LAAKIIKVKS AKDREDVKNE INIMNQLSHV NLIQLYDAFE SKHSCTLVME YVDGGELFDR 

       610        620        630        640        650        660 
ITDEKYHLTE LDVVLFTRQI CEGVHYLHQH YILHLDLKPE NILCVNQTGH QIKIIDFGLA 

       670        680        690        700        710        720 
RRYKPREKLK VNFGTPEFLA PEVVNYEFVS FPTDMWSVGV ITYMLLSGLS PFLGETDAET 

       730        740        750        760        770        780 
MNFIVNCSWD FDADTFEGLS EEAKDFVSRL LVKEKSCRMS ATQCLKHEWL NNLPAKASRS 

       790        800        810 
KTRLKSQLLL QKYIAQRKWK KHFYVVTAAN RLRKFPTSP 

« Hide

Isoform 2 [UniParc].

Checksum: 4AD65710D538D28B
Show »

FASTA47852,723

References

« Hide 'large scale' references
[1]"The cardiac-MyBP-C associated Ca/CaM kinase is a novel MLCK with cardiac-specific domains."
Mues A., Seidel R., Gautel M.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-180.
Tissue: Cardiac myocyte.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Tongue.
[3]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1), VARIANT LEU-180.
[6]"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: TISSUE SPECIFICITY.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-390.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ247087 mRNA. Translation: CAC42766.1. Different initiation.
AK299443 mRNA. Translation: BAH13034.1.
AB451455 mRNA. Translation: BAG70269.1.
AC007225 Genomic DNA. No translation available.
BC109097 mRNA. Translation: AAI09098.2. Different initiation.
RefSeqNP_872299.2. NM_182493.2.
XP_005256292.1. XM_005256235.2.
UniGeneHs.130465.

3D structure databases

ProteinModelPortalQ32MK0.
SMRQ32MK0. Positions 491-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124881. 4 interactions.
IntActQ32MK0. 2 interactions.
STRING9606.ENSP00000378288.

Chemistry

BindingDBQ32MK0.
ChEMBLCHEMBL4627.
GuidetoPHARMACOLOGY2110.

PTM databases

PhosphoSiteQ32MK0.

Polymorphism databases

DMDM254763411.

Proteomic databases

PaxDbQ32MK0.
PRIDEQ32MK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394809; ENSP00000378288; ENSG00000140795. [Q32MK0-3]
ENST00000536476; ENSP00000439297; ENSG00000140795. [Q32MK0-4]
GeneID91807.
KEGGhsa:91807.
UCSCuc002eei.4. human. [Q32MK0-3]
uc002eej.1. human. [Q32MK0-4]

Organism-specific databases

CTD91807.
GeneCardsGC16M046736.
HGNCHGNC:29826. MYLK3.
HPAHPA040258.
MIM612147. gene.
neXtProtNX_Q32MK0.
PharmGKBPA162396375.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG080416.
InParanoidQ32MK0.
KOK00907.
OMAFRMVVAV.
OrthoDBEOG73FQMV.
PhylomeDBQ32MK0.
TreeFamTF314166.

Enzyme and pathway databases

SignaLinkQ32MK0.

Gene expression databases

BgeeQ32MK0.
CleanExHS_MYLK3.
GenevestigatorQ32MK0.

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

GeneWikiMYLK3.
GenomeRNAi91807.
NextBio77465.
PROQ32MK0.
SOURCESearch...

Entry information

Entry nameMYLK3_HUMAN
AccessionPrimary (citable) accession number: Q32MK0
Secondary accession number(s): B5BUL9 expand/collapse secondary AC list , B7Z5U8, Q32MK1, Q96DV1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM