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Protein

Myosin light chain kinase, smooth muscle

Gene

Mylk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca2+ entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells.9 Publications

Catalytic activityi

ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1515 – 15151ATPPROSITE-ProRule annotation
Active sitei1607 – 16071Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1492 – 15009ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • myosin light chain kinase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

Actin-binding, ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.18. 3474.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin light chain kinase, smooth muscle (EC:2.7.11.18)
Short name:
MLCK
Short name:
smMLCK
Alternative name(s):
Kinase-related protein
Short name:
KRP
Telokin
Cleaved into the following chain:
Gene namesi
Name:MylkImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:894806. Mylk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Mice lacking isoform 1 show a reduced flow-mediated dilation of small mesenteric arteries but no significant changes in main cardiovascular function. Increased survival from burn. Prevention of epithelial MLC phosphorylation, tight junction disruption, protein leak, and diarrhea following T-cell activation.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19411941Myosin light chain kinase, smooth musclePRO_0000233949Add
BLAST
Chaini1 – 19341934Myosin light chain kinase, smooth muscle, deglutamylated formPRO_0000403732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi177 ↔ 228PROSITE-ProRule annotation
Modified residuei226 – 2261Phosphotyrosine; by ABL1By similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineCombined sources
Disulfide bondi423 ↔ 475PROSITE-ProRule annotation
Modified residuei452 – 4521Phosphotyrosine; by ABL1 and SRCBy similarity
Disulfide bondi523 ↔ 571PROSITE-ProRule annotation
Disulfide bondi730 ↔ 793PROSITE-ProRule annotation
Modified residuei780 – 7801Phosphotyrosine; by ABL1By similarity
Modified residuei935 – 9351PhosphoserineCombined sources
Disulfide bondi1141 ↔ 1192PROSITE-ProRule annotation
Modified residuei1460 – 14601PhosphoserineCombined sources
Modified residuei1471 – 14711Phosphotyrosine; by ABL1By similarity
Modified residuei1597 – 15971Phosphotyrosine; by ABL1By similarity
Modified residuei1657 – 16571Phosphotyrosine; by ABL1By similarity
Modified residuei1781 – 17811PhosphoserineCombined sources
Modified residuei1782 – 17821PhosphoserineCombined sources
Modified residuei1794 – 17941PhosphoserineBy similarity
Modified residuei1795 – 17951PhosphoserineCombined sources
Modified residuei1798 – 17981PhosphoserineCombined sources
Modified residuei1800 – 18001PhosphothreonineCombined sources
Modified residuei1801 – 18011PhosphoserineCombined sources
Disulfide bondi1852 ↔ 1904PROSITE-ProRule annotation

Post-translational modificationi

Can probably be down-regulated by phosphorylation. Tyrosine phosphorylation by ABL1 increases kinase activity, reverses MLCK-mediated inhibition of Arp2/3-mediated actin polymerization, and enhances CTTN-binding. Phosphorylation by SRC at Tyr-452 promotes CTTN binding (By similarity).By similarity
The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and AGBL4/CCP6, leading to the formation of Myosin light chain kinase, smooth muscle, deglutamylated form. The consequences of C-terminal deglutamylation are unknown (PubMed:21074048).1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ6PDN3.
MaxQBiQ6PDN3.
PaxDbiQ6PDN3.
PeptideAtlasiQ6PDN3.
PRIDEiQ6PDN3.

PTM databases

iPTMnetiQ6PDN3.
PhosphoSiteiQ6PDN3.

Expressioni

Tissue specificityi

Smooth muscle isoform expressed in all tissues with highest levels in bladder, uterus, vas deferens, colon, ileum, and tracheae. Isoform 1 expressed in lung, bladder, and vas deferens. Telokin expressed in smooth muscle cells of uterus, vas deferens, bladder, colon, kidney, ureter, ovary and trachea.2 Publications

Developmental stagei

Isoform 1 ubiquitously expressed in E14.5 embryos with highest levels in some areas of the developing brain, the lower gastrointestinal tract as well as certain blood vessels. Primary cultures of endothelial cells lose high level expression of Smooth muscle isoform with increasing number of passages. Telokin expressed in embryonic gut from E11.5 with highest level in E15.5. Also expressed in developing bronchi from E13.5. High levels in E15.5 bladder, ureter, urethra and rectum. Telokin expression is induced in reproductive tract during postnatal development.2 Publications

Gene expression databases

CleanExiMM_MYLK.

Interactioni

Subunit structurei

All isoforms including Telokin bind calmodulin. Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 (By similarity). Interacts with SVIL and PTK2B/PYK2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Patz1Q9JMG93EBI-647412,EBI-647451

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ6PDN3. 21 interactions.
MINTiMINT-1849579.
STRINGi10090.ENSMUSP00000023538.

Structurei

3D structure databases

ProteinModelPortaliQ6PDN3.
SMRiQ6PDN3. Positions 3-291, 353-810, 1102-1924.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12290Ig-like C2-type 1Sequence analysisAdd
BLAST
Domaini156 – 24489Ig-like C2-type 2Sequence analysisAdd
BLAST
Domaini402 – 48584Ig-like C2-type 3Sequence analysisAdd
BLAST
Domaini502 – 58786Ig-like C2-type 4Sequence analysisAdd
BLAST
Domaini611 – 69989Ig-like C2-type 5Sequence analysisAdd
BLAST
Domaini709 – 809101Ig-like C2-type 6Sequence analysisAdd
BLAST
Repeati856 – 883281-1By similarityAdd
BLAST
Repeati884 – 911281-2By similarityAdd
BLAST
Repeati912 – 939281-3By similarityAdd
BLAST
Repeati940 – 966271-4By similarityAdd
BLAST
Repeati967 – 985191-5; truncatedAdd
BLAST
Repeati990 – 1002132-1By similarityAdd
BLAST
Repeati1003 – 1014122-2By similarityAdd
BLAST
Repeati1015 – 1026122-3By similarityAdd
BLAST
Repeati1027 – 1038122-4By similarityAdd
BLAST
Repeati1039 – 1049112-5By similarityAdd
BLAST
Domaini1120 – 120889Ig-like C2-type 7Sequence analysisAdd
BLAST
Domaini1260 – 134889Ig-like C2-type 8Sequence analysisAdd
BLAST
Domaini1356 – 144994Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini1486 – 1741256Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1831 – 192090Ig-like C2-type 9Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni856 – 9851305 X 28 AA approximate tandem repeatsAdd
BLAST
Regioni911 – 95141Actin-binding (calcium/calmodulin-sensitive)By similarityAdd
BLAST
Regioni936 – 95116Calmodulin-bindingBy similarityAdd
BLAST
Regioni990 – 1049605 X 12 AA approximate tandem repeatsAdd
BLAST
Regioni1048 – 1482435Actin-binding (calcium/calmodulin-insensitive)By similarityAdd
BLAST
Regioni1733 – 179664Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1918 – 194124Glu-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 9 Ig-like C2-type (immunoglobulin-like) domains.Sequence analysis
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
HOVERGENiHBG052551.
InParanoidiQ6PDN3.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. AlignAdd to basket

Isoform 11 Publication (identifier: Q6PDN3-1) [UniParc]FASTAAdd to basket

Also known as: Non muscle isozyme1 Publication

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.

« Hide

        10         20         30         40         50
MGDVKLFASS HMSKTSHSVD PSKVSSMPLT EAPAFILPPR NLCVKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRKG QAITNGGRFL LDCGVRGTFS LVIHTVREED
110 120 130 140 150
KGKYTCEASN GSGARQVTVE LTVEGNSMKK RDQPVLSKAS GFPGETRPSI
160 170 180 190 200
WGECPPKFAT KLGRAVVKEG QMWRFSCKIT GRPPPQVTWL KGNVPLQPSA
210 220 230 240 250
RVSMSEKNGM QILEIRGVTR DDLGVYTCMV VNGSGKASMS AELSIPGLDN
260 270 280 290 300
ASRLAVRGTK APSPDIRKEV TNGVSKDPET VAESKNCPSP QRSGSSARAT
310 320 330 340 350
NSHLKSPQEP KPKLCEDAPR KVPQSSILQK STSTITLQAL KVQPEARVPA
360 370 380 390 400
IGSFSPGEDR KSLAAPQQAT LPTRQSSLGG SVGNKFVTGN IPRESQREST
410 420 430 440 450
FPRFESQPQS QEVTEGQTVK FICEVSGIPK PDVGWFLEGI PVRRREGITE
460 470 480 490 500
VYEDGVSHHL CLLRARTRDS RKYSCTASNS LGQVSCSWSL LVDRPNLAQT
510 520 530 540 550
APSFSSVLKD SVVIEGQDFV LRCSVQGTPA PRVTWLLNGQ PIQFAHSICE
560 570 580 590 600
AGVAELHIQD ALPEDRGTYT CLAENAMGQV SCSATVTVQE KKGEGEREHR
610 620 630 640 650
LSPARSKPIA PIFLQGLSDL KVMDGSQVTM TVQVSGNPPP EVIWLHDGNE
660 670 680 690 700
IQESEDFHFE QKGGWHSLCI QEVFPEDTGT YTCEAWNSAG EVRTRAVLTV
710 720 730 740 750
QEPHDGTQPW FISKPRSVTA TLGQSVLISC AIAGDPFPTV HWLRDGRALS
760 770 780 790 800
KDSGHFELLQ NEDVFTLVLK NVQPWHAGQY EILLKNRVGE CSCQVSLMLH
810 820 830 840 850
NSPSRAPPRG REPASCEGLC GGGGVGAHGD GDRHGTLRPC WPARGQGWPE
860 870 880 890 900
EEDGEDVRGL LKRRVETRLH TEEAIRQQEV GQLDFRDLLG KKVSTKTVSE
910 920 930 940 950
DDLKDIPAEQ MDFRANLQRQ VKPKTISEEE RKVHSPQQVD FRSVLAKKGT
960 970 980 990 1000
PKTPVPEKAP PKAATPDFRS VLGGKKKSPS ENGGNSAEVL NVKAGESPTP
1010 1020 1030 1040 1050
AGDAQAIGAL KPVGNAKPAE TPKPIGNAKP TETLKPVGNT KPAETLKPIA
1060 1070 1080 1090 1100
NAQPSGSLKP VTNAQPAEPQ KPVGNAKSAE TSKPAGKEEV KEVKNDVNCK
1110 1120 1130 1140 1150
KGQVGATGNE KRPESQGSAP VFKEKLQDVH VAEGEKLLLQ CQVISDPPAT
1160 1170 1180 1190 1200
VTWSLNGKTL KTTKFIVLAQ EGSRFSVSIE KALPEDRGLY KCVAKNSAGQ
1210 1220 1230 1240 1250
AECSCQVTVD DAQTSENTKA PEMKSRRPKS SLPPVLGTES DATVKKKPAP
1260 1270 1280 1290 1300
KTPTKAAMPP QIIQFPEDQK VRAGEPVELF GKVAGTQPIT CKWMKFRKQI
1310 1320 1330 1340 1350
QESEHIKVEN GESGSKLTIL AARQEHCGCY TLVVENKLGS RQAQVNLTVV
1360 1370 1380 1390 1400
DKPDPPAGTP CASDIRSSSL TLSWYGSSYD GGSAVQSYNV EIWDTEDKVW
1410 1420 1430 1440 1450
KELATCRSTS FNVQDLLPDR EYKFRVRAVN VYGTSEPSQE SELTAVGEKP
1460 1470 1480 1490 1500
EEPKDEVEVS DDDEKEPEVD YRTVTVNTEQ KVSDVYDIEE RLGSGKFGQV
1510 1520 1530 1540 1550
FRLVEKKTGK IWAGKFFKAY SAKEKDNIRQ EISIMNCLHH PKLVQCVDAF
1560 1570 1580 1590 1600
EEKANIVMVL EIVSGGELFE RIIDEDFELT ERECIKYMRQ ISEGVEYIHK
1610 1620 1630 1640 1650
QGIVHLDLKP ENIMCVNKTG TRIKLIDFGL ARRLENAGSL KVLFGTPEFV
1660 1670 1680 1690 1700
APEVINYEPI GYATDMWSIG VICYILVSGL SPFMGDNDNE TLANVTSATW
1710 1720 1730 1740 1750
DFDDEAFDEI SDDAKDFISN LLKKDMKNRL DCTQCLQHPW LMKDTKNMEA
1760 1770 1780 1790 1800
KKLSKDRMKK YMARRKWQKT GNAVRAIGRL SSMAMISGLS GRKSSTGSPT
1810 1820 1830 1840 1850
SPINAEKLES EDDVSQAFLE AVAEEKPHVK PYFSKTIRDL EVVEGSAARF
1860 1870 1880 1890 1900
DCKIEGYPDP EVVWFKDDQS IRESRHFQID YDEDGNCSLI ISDVCGDDDA
1910 1920 1930 1940
KYTCKAVNSL GEATCTAELI VETMEEGEGE EGGEEEEEEE E
Length:1,941
Mass (Da):212,925
Last modified:May 2, 2006 - v3
Checksum:i7FF12C60F1BDFFDD
GO
Isoform 21 Publication (identifier: Q6PDN3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1254: Missing.
     1255-1256: KA → MQ

Note: Produced by alternative promoter usage and alternative splicing. No experimental confirmation available.
Show »
Length:687
Mass (Da):77,433
Checksum:iDCCF826A8ABA42B5
GO
Isoform 3 (identifier: Q6PDN3-3) [UniParc]FASTAAdd to basket

Also known as: Smooth muscle isozyme

The sequence of this isoform differs from the canonical sequence as follows:
     1-910: Missing.

Note: Produced by alternative initiation at Met-911 of isoform 1.
Show »
Length:1,031
Mass (Da):113,703
Checksum:iD9435CF18C0E4337
GO
Isoform 4 (identifier: Q6PDN3-4) [UniParc]FASTAAdd to basket

Also known as: Telokin

The sequence of this isoform differs from the canonical sequence as follows:
     1-1782: Missing.

Note: Produced by alternative initiation at Met-1783 of isoform 1.
Show »
Length:159
Mass (Da):17,529
Checksum:i7EFDC75F450F3B6D
GO

Sequence cautioni

The sequence AAH58610.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAO85807.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731W → G (PubMed:11832329).Curated
Sequence conflicti173 – 1731W → G (PubMed:11472067).Curated
Sequence conflicti252 – 2521S → A in AAK53241 (PubMed:11472067).Curated
Sequence conflicti471 – 4722RK → GR (PubMed:11832329).Curated
Sequence conflicti471 – 4722RK → GR (PubMed:11472067).Curated
Sequence conflicti478 – 4781S → T in AAO85807 (PubMed:11832329).Curated
Sequence conflicti482 – 4821G → A in AAO85807 (PubMed:11832329).Curated
Sequence conflicti666 – 6672HS → TP in AAO85807 (PubMed:11832329).Curated
Sequence conflicti677 – 6771D → S in AAO85807 (PubMed:11832329).Curated
Sequence conflicti749 – 7502LS → SP in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1004 – 10041A → G in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1038 – 10381G → A in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1106 – 11061A → R in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1174 – 11818RFSVSIEK → TFLCLHRE in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1210 – 12101D → A in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1289 – 12891I → T in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1340 – 13401Missing in BAE36678 (PubMed:16141072).Curated
Sequence conflicti1409 – 14091T → H in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1657 – 16571Y → H in AAH58610 (PubMed:15489334).Curated
Sequence conflicti1661 – 16611G → R in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1678 – 16781S → R in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1706 – 17061A → E in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1732 – 17354CTQC → STHG in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1825 – 18251E → K in AAO85807 (PubMed:11832329).Curated
Sequence conflicti1888 – 18881S → T in AAG34169 (PubMed:11121372).Curated
Sequence conflicti1941 – 19411Missing in AAH58610 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17821782Missing in isoform 4. 1 PublicationVSP_018848Add
BLAST
Alternative sequencei1 – 12541254Missing in isoform 2. 1 PublicationVSP_052002Add
BLAST
Alternative sequencei1 – 910910Missing in isoform 3. 1 PublicationVSP_018847Add
BLAST
Alternative sequencei1255 – 12562KA → MQ in isoform 2. 1 PublicationVSP_052003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237727 mRNA. Translation: AAO85808.1.
AF314149 mRNA. Translation: AAG34169.1.
AY237726 mRNA. Translation: AAO85807.1. Different initiation.
AK162008 mRNA. Translation: BAE36678.1.
BC034209 mRNA. Translation: AAH34209.1.
BC045197 mRNA. Translation: AAH45197.1.
BC058610 mRNA. Translation: AAH58610.2. Different initiation.
AF335470 Genomic DNA. Translation: AAK53241.1.
UniGeneiMm.33360.

Genome annotation databases

UCSCiuc007zbe.1. mouse. [Q6PDN3-1]
uc007zbh.1. mouse. [Q6PDN3-4]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237727 mRNA. Translation: AAO85808.1.
AF314149 mRNA. Translation: AAG34169.1.
AY237726 mRNA. Translation: AAO85807.1. Different initiation.
AK162008 mRNA. Translation: BAE36678.1.
BC034209 mRNA. Translation: AAH34209.1.
BC045197 mRNA. Translation: AAH45197.1.
BC058610 mRNA. Translation: AAH58610.2. Different initiation.
AF335470 Genomic DNA. Translation: AAK53241.1.
UniGeneiMm.33360.

3D structure databases

ProteinModelPortaliQ6PDN3.
SMRiQ6PDN3. Positions 3-291, 353-810, 1102-1924.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6PDN3. 21 interactions.
MINTiMINT-1849579.
STRINGi10090.ENSMUSP00000023538.

Protein family/group databases

MEROPSiI43.001.

PTM databases

iPTMnetiQ6PDN3.
PhosphoSiteiQ6PDN3.

Proteomic databases

EPDiQ6PDN3.
MaxQBiQ6PDN3.
PaxDbiQ6PDN3.
PeptideAtlasiQ6PDN3.
PRIDEiQ6PDN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc007zbe.1. mouse. [Q6PDN3-1]
uc007zbh.1. mouse. [Q6PDN3-4]

Organism-specific databases

MGIiMGI:894806. Mylk.

Phylogenomic databases

eggNOGiKOG0613. Eukaryota.
ENOG410XQFD. LUCA.
HOVERGENiHBG052551.
InParanoidiQ6PDN3.

Enzyme and pathway databases

BRENDAi2.7.11.18. 3474.

Miscellaneous databases

ChiTaRSiMylk. mouse.
PROiQ6PDN3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MYLK.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR10489:SF700. PTHR10489:SF700. 4 hits.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 9 hits.
SM00408. IGc2. 9 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 9 hits.
SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS50835. IG_LIKE. 9 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
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Publicationsi

« Hide 'large scale' publications
  1. "Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle."
    Herring B.P., Dixon S.A., Gallagher P.J.
    Am. J. Physiol. 279:C1656-C1664(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Strain: C3H/HeJ1 Publication.
    Tissue: Cardiac myocyte1 Publication.
  2. "Telokin expression is restricted to smooth muscle tissues during mouse development."
    Herring B.P., Lyons G.E., Hoggatt A.M., Gallagher P.J.
    Am. J. Physiol. 280:C12-C21(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Swiss Webster / NIHImported.
  3. "220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patterns."
    Blue E.K., Goeckeler Z.M., Jin Y., Hou L., Dixon S.A., Herring B.P., Wysolmerski R.B., Gallagher P.J.
    Am. J. Physiol. 282:C451-C460(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C3H/HeJImported.
    Tissue: Cardiac myocyte1 Publication.
  4. "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.
    , 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] (ISOFORM 2).
    Strain: C57BL/6JImported.
    Tissue: Wolffian ductImported.
  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).
    Strain: C3H/HeImported and FVB/NImported.
    Tissue: ColonImported, Mammary glandImported and OsteoblastImported.
  6. "The myosin light chain kinase gene is not duplicated in mouse: partial structure and chromosomal localization of Mylk."
    Giorgi D.G., Ferraz C., Mattei M.-G., Demaille J., Rouquier S.
    Genomics 75:49-56(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1561 (ISOFORM 1).
    Strain: C57BL/6JImported.
  7. "Intestinal infection with Giardia spp. reduces epithelial barrier function in a myosin light chain kinase-dependent fashion."
    Scott K.G.-E., Meddings J.B., Kirk D.R., Lees-Miller S.P., Buret A.G.
    Gastroenterology 123:1179-1190(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GIARDIASIS.
  8. "Deletion of MLCK210 induces subtle changes in vascular reactivity but does not affect cardiac function."
    Ohlmann P., Tesse A., Loichot C., Ralay Ranaivo H., Roul G., Philippe C., Watterson D.M., Haiech J., Andriantsitohaina R.
    Am. J. Physiol. 289:H2342-H2349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Epithelial myosin light chain kinase-dependent barrier dysfunction mediates T cell activation-induced diarrhea in vivo."
    Clayburgh D.R., Barrett T.A., Tang Y., Meddings J.B., Van Eldik L.J., Watterson D.M., Clarke L.L., Mrsny R.J., Turner J.R.
    J. Clin. Invest. 115:2702-2715(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTESTINAL BARRIER DYSFUNCTION.
  10. "Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery."
    Takizawa N., Ikebe R., Ikebe M., Luna E.J.
    J. Cell Sci. 120:3792-3803(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SVIL.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-1782 AND SER-1798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "A role for long chain myosin light chain kinase (MLCK-210) in microvascular hyperpermeability during severe burns."
    Reynoso R., Perrin R.M., Breslin J.W., Daines D.A., Watson K.D., Watterson D.M., Wu M.H., Yuan S.
    Shock 28:589-595(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MICROVASCULAR HYPERPERMEABILITY DURING SEVERE BURNS, DISRUPTION PHENOTYPE.
  13. "Myosin light chain kinase is central to smooth muscle contraction and required for gastrointestinal motility in mice."
    He W.-Q., Peng Y.-J., Zhang W.-C., Lv N., Tang J., Chen C., Zhang C.-H., Gao S., Chen H.-Q., Zhi G., Feil R., Kamm K.E., Stull J.T., Gao X., Zhu M.-S.
    Gastroenterology 135:610-620(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SMOOTH MUSCLE CONTRACTION.
  14. "Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins."
    Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.
    Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PTK2B/PYK2 KINASE, INTERACTION WITH PTK2B/PYK2.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-355; SER-935; SER-1460; SER-1781; SER-1782; SER-1795; SER-1798; THR-1800 AND SER-1801, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  16. Cited for: DEGLUTAMYLATION.
  17. Cited for: FUNCTION IN TONIC AIRWAY SMOOTH MUSCLE CONTRACTION.
  18. "MLCK-dependent exchange and actin binding region-dependent anchoring of ZO-1 regulate tight junction barrier function."
    Yu D., Marchiando A.M., Weber C.R., Raleigh D.R., Wang Y., Shen L., Turner J.R.
    Proc. Natl. Acad. Sci. U.S.A. 107:8237-8241(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TIGHT JUNCTION REGULATION.

Entry informationi

Entry nameiMYLK_MOUSE
AccessioniPrimary (citable) accession number: Q6PDN3
Secondary accession number(s): Q3TSJ7
, Q80UX0, Q80YN7, Q80YN8, Q8K026, Q924D2, Q9ERD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: July 6, 2016
This is version 115 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.