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Myosin light chain kinase, smooth muscle (MLCK) (EC 2.7.11.18) (Telokin) [Cleaved into: Myosin light chain kinase, smooth muscle, deglutamylated form]

 MYLK_CHICK              Reviewed;        1906 AA.
P11799; P19038; Q549S2;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
05-DEC-2018, entry version 189.
RecName: Full=Myosin light chain kinase, smooth muscle;
Short=MLCK;
EC=2.7.11.18;
AltName: Full=Telokin;
Contains:
RecName: Full=Myosin light chain kinase, smooth muscle, deglutamylated form;
Name=Mylk;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7589469; DOI=10.1016/0014-5793(95)01048-J;
Watterson D.M., Collinge M., Lukas T.J., van Eldik L.J., Birukov K.G.,
Stepanova O.V., Shirinsky V.P.;
"Multiple gene products are produced from a novel protein kinase
transcription region.";
FEBS Lett. 373:217-220(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2315320; DOI=10.1073/pnas.87.6.2284;
Olson N.J., Pearson R.B., Needleman D.S., Hurwitz M.J., Kemp B.E.,
Means A.R.;
"Regulatory and structural motifs of chicken gizzard myosin light
chain kinase.";
Proc. Natl. Acad. Sci. U.S.A. 87:2284-2288(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=9706877;
DOI=10.1002/(SICI)1097-4644(19980901)70:3<402::AID-JCB13>3.3.CO;2-4;
Birukov K.G., Schavocky J.P., Shirinsky V.P., Van Eldik L.J.,
Watterson D.M.;
"The organization of the genetic locus for chicken myosin light chain
kinase is complex: multiple proteins are encoded and exhibit
differential expression and localization.";
J. Cell. Biochem. 70:402-413(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 649-1906, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fibroblast;
PubMed=2202734; DOI=10.1083/jcb.111.3.1107;
Shoemaker M.O., Lau W., Shattuck R.L., Kwiatkowski A.P.,
Matrisian P.E., Guerra-Santos L., Wilson E., Lukas T.J.,
van Eldik L.J., Watterson D.M.;
"Use of DNA sequence and mutant analyses and antisense
oligodeoxynucleotides to examine the molecular basis of nonmuscle
myosin light chain kinase autoinhibition, calmodulin recognition, and
activity.";
J. Cell Biol. 111:1107-1125(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1906.
TISSUE=Gizzard;
PubMed=3030394; DOI=10.1021/bi00374a007;
Guerriero V. Jr., Russo M.A., Olson N.J., Putkey J.A., Means A.R.;
"Domain organization of chicken gizzard myosin light chain kinase
deduced from a cloned cDNA.";
Biochemistry 25:8372-8381(1986).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1906 (ISOFORM 3).
TISSUE=Gizzard;
PubMed=1444462; DOI=10.1016/0003-9861(92)90270-7;
Yoshikai S., Ikebe M.;
"Molecular cloning of the chicken gizzard telokin gene and cDNA.";
Arch. Biochem. Biophys. 299:242-247(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1750-1906 (ISOFORM 3).
PubMed=1373815; DOI=10.1128/MCB.12.5.2359;
Collinge M., Matrisian P.E., Zimmer W.E., Shattuck R.L., Lukas T.J.,
van Eldik L.J., Watterson D.M.;
"Structure and expression of a calcium-binding protein gene contained
within a calmodulin-regulated protein kinase gene.";
Mol. Cell. Biol. 12:2359-2371(1992).
[8]
PROTEIN SEQUENCE OF 1775-1789, ACETYLATION, DEGLUTAMYLATION,
PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9283094; DOI=10.1021/bi970752e;
Rusconi F., Potier M.C., Le Caer J.P., Schmitter J.M., Rossier J.;
"Characterization of the chicken telokin heterogeneity by time-of-
flight mass spectrometry.";
Biochemistry 36:11021-11026(1997).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1762 AND SER-1768, AND
MUTAGENESIS OF SER-1762 AND SER-1768.
PubMed=12176732; DOI=10.1152/ajpcell.00501.2001;
Komatsu S., Miyazaki K., Tuft R.A., Ikebe M.;
"Translocation of telokin by cGMP signaling in smooth muscle cells.";
Am. J. Physiol. 283:C752-C761(2002).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1731-1749 IN COMPLEX WITH
CALM1 AND CALCIUM.
PubMed=10194305; DOI=10.1021/bi9821263;
Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F.,
Watterson D.M.;
"Analysis of the functional coupling between calmodulin's calcium
binding and peptide recognition properties.";
Biochemistry 38:3936-3947(1999).
[11]
ERRATUM.
PubMed=10529260; DOI=10.1021/bi9950894;
Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F.,
Watterson D.M.;
Biochemistry 38:14117-14118(1999).
-!- FUNCTION: Phosphorylates a specific serine in the N-terminus of a
myosin light chain, which leads to the formation of
calmodulin/MLCK signal transduction complexes which allow
selective transduction of calcium signals.
-!- CATALYTIC ACTIVITY:
Reaction=[myosin light chain]-L-serine + ATP = [myosin light
chain]-O-phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:22004,
Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.18;
-!- CATALYTIC ACTIVITY:
Reaction=[myosin light chain]-L-threonine + ATP = [myosin light
chain]-O-phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:53900,
Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.18;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Activated by phosphorylation on Tyr-478.
Isoforms which lack this tyrosine residue are not regulated in
this way. All catalytically active isoforms require binding to
calcium and calmodulin for activation.
-!- SUBUNIT: All isoforms including Telokin bind calmodulin.
{ECO:0000269|PubMed:10194305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12176732}. Membrane
{ECO:0000269|PubMed:12176732}. Note=Telokin is cytosolic and can
translocate to the membrane upon stimulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=3;
Name=1; Synonyms=MLCK-108, Smooth-muscle;
IsoId=P11799-1; Sequence=Displayed;
Name=2; Synonyms=MLCK-210, Non-muscle;
IsoId=P11799-2; Sequence=VSP_018851;
Name=3; Synonyms=Telokin;
IsoId=P11799-3; Sequence=VSP_018852;
-!- TISSUE SPECIFICITY: Isoform telokin is expressed in gizzard,
heart, lung, intestine, and skeletal muscle although the levels of
the expression in the latter were much less than that in the
gizzard.
-!- PTM: The C-terminus is deglutamylated, leading to the formation of
Myosin light chain kinase, smooth muscle, deglutamylated form. The
C-terminus is variable, with one to five C-terminal glutamyl
residues being removed producing five forms differring in their
number of C-terminal glutamyl residues.
{ECO:0000269|PubMed:9283094}.
-!- PTM: Acetylated. {ECO:0000269|PubMed:9283094}.
-!- PTM: Phosphorylation of telokin by PKG has no significant effect
on its myosin binding activity, but promotes translocation to the
membrane. {ECO:0000269|PubMed:12176732,
ECO:0000269|PubMed:9283094}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
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EMBL; X52876; CAA37056.1; -; mRNA.
EMBL; X52876; CAA37057.1; -; mRNA.
EMBL; X52876; CAA37058.1; -; mRNA.
EMBL; M31048; AAA49069.1; -; mRNA.
EMBL; M14953; AAA69964.1; -; mRNA.
EMBL; AF045285; AAC29031.1; -; Genomic_DNA.
EMBL; AF045255; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045256; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045257; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045260; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045259; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045258; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045261; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045263; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045265; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045274; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045273; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045272; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045271; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045270; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045269; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045268; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045267; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045266; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045283; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045282; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045281; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045280; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045279; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045278; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045277; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045276; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045275; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045284; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045264; AAC29031.1; JOINED; Genomic_DNA.
EMBL; AF045262; AAC29031.1; JOINED; Genomic_DNA.
EMBL; M96655; AAA49083.1; -; mRNA.
EMBL; M88283; AAA48647.1; -; mRNA.
EMBL; M88284; AAB53768.1; -; Genomic_DNA.
PIR; S68235; S68235.
RefSeq; XP_015145280.1; XM_015289794.1.
UniGene; Gga.4091; -.
PDB; 1CDL; X-ray; 2.00 A; E/F/G/H=1730-1749.
PDB; 1QS7; X-ray; 1.80 A; B/D=1731-1749.
PDB; 1QTX; X-ray; 1.65 A; B=1731-1749.
PDB; 1VRK; X-ray; 1.90 A; B=1731-1749.
PDB; 2O5G; X-ray; 1.08 A; B=1730-1748.
PDB; 3EVU; X-ray; 1.75 A; A=1731-1749.
PDB; 3EVV; X-ray; 2.60 A; A=1731-1749.
PDB; 3O77; X-ray; 2.35 A; A=1730-1749.
PDB; 3O78; X-ray; 2.60 A; A/B=1731-1749.
PDB; 4OY4; X-ray; 2.03 A; A=1715-1725, A=1731-1749.
PDBsum; 1CDL; -.
PDBsum; 1QS7; -.
PDBsum; 1QTX; -.
PDBsum; 1VRK; -.
PDBsum; 2O5G; -.
PDBsum; 3EVU; -.
PDBsum; 3EVV; -.
PDBsum; 3O77; -.
PDBsum; 3O78; -.
PDBsum; 4OY4; -.
ProteinModelPortal; P11799; -.
SMR; P11799; -.
BioGrid; 676694; 1.
IntAct; P11799; 3.
MINT; P11799; -.
STRING; 9031.ENSGALP00000019112; -.
BindingDB; P11799; -.
ChEMBL; CHEMBL3062; -.
iPTMnet; P11799; -.
PaxDb; P11799; -.
PRIDE; P11799; -.
eggNOG; KOG0613; Eukaryota.
eggNOG; ENOG410XQFD; LUCA.
HOGENOM; HOG000049287; -.
HOVERGEN; HBG052551; -.
PhylomeDB; P11799; -.
BRENDA; 2.7.11.18; 1306.
EvolutionaryTrace; P11799; -.
PRO; PR:P11799; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031430; C:M band; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0030017; C:sarcomere; IBA:GO_Central.
GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
GO; GO:0004687; F:myosin light chain kinase activity; IEA:UniProtKB-EC.
GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
GO; GO:0048739; P:cardiac muscle fiber development; IBA:GO_Central.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IBA:GO_Central.
GO; GO:0055003; P:cardiac myofibril assembly; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IBA:GO_Central.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IBA:GO_Central.
CDD; cd00063; FN3; 1.
CDD; cd14191; STKc_MLCK1; 1.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR015725; MLCK1_kinase_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00041; fn3; 1.
Pfam; PF07679; I-set; 9.
Pfam; PF00069; Pkinase; 1.
SMART; SM00060; FN3; 1.
SMART; SM00409; IG; 9.
SMART; SM00408; IGc2; 9.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48726; SSF48726; 9.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50835; IG_LIKE; 9.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative promoter usage; ATP-binding;
Calcium; Calmodulin-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Immunoglobulin domain; Kinase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 1906 Myosin light chain kinase, smooth muscle.
/FTId=PRO_0000024361.
CHAIN 1 1901 Myosin light chain kinase, smooth muscle,
deglutamylated form.
/FTId=PRO_0000424867.
DOMAIN 28 117 Ig-like C2-type 1.
DOMAIN 156 244 Ig-like C2-type 2.
DOMAIN 429 517 Ig-like C2-type 3.
DOMAIN 521 613 Ig-like C2-type 4.
DOMAIN 637 725 Ig-like C2-type 5.
REPEAT 660 676 IIA-1.
REPEAT 693 708 IIB-1.
DOMAIN 735 830 Ig-like C2-type 6.
REPEAT 758 774 IIA-2.
REPEAT 791 807 IIB-2.
REPEAT 970 987 III-1.
REPEAT 999 1016 III-2.
REPEAT 1061 1078 III-3.
DOMAIN 1084 1172 Ig-like C2-type 7.
REPEAT 1107 1123 IIA-3.
REPEAT 1140 1156 IIB-3.
REPEAT 1209 1226 III-4.
DOMAIN 1225 1313 Ig-like C2-type 8.
REPEAT 1281 1297 IIB-4.
DOMAIN 1321 1414 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1453 1708 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 1794 1885 Ig-like C2-type 9.
REPEAT 1817 1833 IIA-4.
REPEAT 1851 1866 IIB-5.
NP_BIND 1459 1467 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 660 1833 4 X repeats, motif IIA.
REGION 693 1866 5 X repeats, motif IIB.
REGION 970 1226 4 X repeats, motif III.
REGION 1317 1364 Motif IA.
REGION 1385 1402 Motif IB.
REGION 1700 1763 Calmodulin-binding.
REGION 1716 1728 Calmodulin autoinhibition (AM13) region.
{ECO:0000255}.
REGION 1730 1749 Calmodulin recognition (RS20) region.
{ECO:0000255}.
COMPBIAS 1896 1906 Poly-Glu.
ACT_SITE 1574 1574 Proton acceptor.
BINDING 1482 1482 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1762 1762 Phosphoserine; by PKG.
{ECO:0000269|PubMed:12176732}.
MOD_RES 1768 1768 Phosphoserine; by MAPK.
{ECO:0000305|PubMed:12176732}.
VAR_SEQ 1 1749 Missing (in isoform 3).
{ECO:0000303|PubMed:1373815,
ECO:0000303|PubMed:1444462}.
/FTId=VSP_018852.
VAR_SEQ 1 934 Missing (in isoform 2).
{ECO:0000303|PubMed:7589469}.
/FTId=VSP_018851.
MUTAGEN 1762 1762 S->A: Decreases membrane translocation.
{ECO:0000269|PubMed:12176732}.
MUTAGEN 1768 1768 S->A: Decreases membrane translocation.
{ECO:0000269|PubMed:12176732}.
CONFLICT 1439 1439 R -> Q (in Ref. 5; AAA49069/AAA69964).
{ECO:0000305}.
CONFLICT 1776 1776 E -> D (in Ref. 8; AA sequence).
{ECO:0000305}.
STRAND 1719 1722 {ECO:0000244|PDB:4OY4}.
HELIX 1731 1747 {ECO:0000244|PDB:2O5G}.
STRAND 1753 1758 {ECO:0000244|PDB:3EVU}.
HELIX 1759 1761 {ECO:0000244|PDB:3EVU}.
SEQUENCE 1906 AA; 210446 MW; AD7D8A3B69EE3363 CRC64;
MGDVKLVTST RVSKTSLTLS PSVPAEAPAF TLPPRNIRVQ LGATARFEGK VRGYPEPQIT
WYRNGHPLPE GDHYVVDHSI RGIFSLVIKG VQEGDSGKYT CEAANDGGVR QVTVELTVEG
NSLKKYSLPS SAKTPGGRLS VPPVEHRPSI WGESPPKFAT KPNRVVVREG QTGRFSCKIT
GRPQPQVTWT KGDIHLQQNE RFNMFEKTGI QYLEIQNVQL ADAGIYTCTV VNSAGKASVS
AELTVQGPDK TDTHAQPLCM PPKPTTLATK AIENSDFKQA TSNGIAKELK STSTELMVET
KDRLSAKKET FYTSREAKDG KQGQNQEANA VPLQESRGTK GPQVLQKTSS TITLQAVKAQ
PEPKAEPQTT FIRQAEDRKR TVQPLMTTTT QENPSLTGQV SPRSRETENR AGVRKSVKEE
KREPLGIPPQ FESRPQSLEA SEGQEIKFKS KVSGKPKPDV EWFKEGVPIK TGEGIQIYEE
DGTHCLWLKK ACLGDSGSYS CAAFNPRGQT STSWLLTVKR PKVEEVAPCF SSVLKGCTVS
EGQDFVLQCY VGGVPVPEIT WLLNEQPIQY AHSTFEAGVA KLTVQDALPE DDGIYTCLAE
NNAGRASCSA QVTVKEKKSS KKAEGTQAAK LNKTFAPIFL KGLTDLKVMD GSQVIMTVEV
SANPCPEIIW LHNGKEIQET EDFHFEKKGN EYSLYIQEVF PEDTGKYTCE AWNELGETQT
QATLTVQEPQ DGIQPWFISK PRSVTAAAGQ NVLISCAIAG DPFPTVHWFK DGQEITPGTG
CEILQNEDIF TLILRNVQSR HAGQYEIQLR NQVGECSCQV SLMLRESSAS RAEMLRDGRE
SASSGERRDG GNYGALTFGR TSGFKKSSSE TRAAEEEQED VRGVLKRRVE TREHTEESLR
QQEAEQLDFR DILGKKVSTK SFSEEDLKEI PAEQMDFRAN LQRQVKPKTL SEEERKVHAP
QQVDFRSVLA KKGTPKTPLP EKVPPPKPAV TDFRSVLGAK KKPPAENGSA STPAPNARAG
SEAQNATPNS EAPAPKPVVK KEEKNDRKCE HGCAVVDGGI IGKKAENKPA ASKPTPPPSK
GTAPSFTEKL QDAKVADGEK LVLQCRISSD PPASVSWTLD SKAIKSSKSI VISQEGTLCS
LTIEKVMPED GGEYKCIAEN AAGKAECACK VLVEDTSSTK AAKPAEKKTK KPKTTLPPVL
STESSEATVK KKPAPKTPPK AATPPQITQF PEDRKVRAGE SVELFAKVVG TAPITCTWMK
FRKQIQENEY IKIENAENSS KLTISSTKQE HCGCYTLVVE NKLGSRQAQV NLTVVDKPDP
PAGTPCASDI RSSSLTLSWY GSSYDGGSAV QSYTVEIWNS VDNKWTDLTT CRSTSFNVQD
LQADREYKFR VRAANVYGIS EPSQESEVVK VGEKQEEELK EEEAELSDDE GKETEVNYRT
VTINTEQKVS DVYNIEERLG SGKFGQVFRL VEKKTGKVWA GKFFKAYSAK EKENIRDEIS
IMNCLHHPKL VQCVDAFEEK ANIVMVLEMV SGGELFERII DEDFELTERE CIKYMRQISE
GVEYIHKQGI VHLDLKPENI MCVNKTGTSI KLIDFGLARR LESAGSLKVL FGTPEFVAPE
VINYEPIGYE TDMWSIGVIC YILVSGLSPF MGDNDNETLA NVTSATWDFD DEAFDEISDD
AKDFISNLLK KDMKSRLNCT QCLQHPWLQK DTKNMEAKKL SKDRMKKYMA RRKWQKTGHA
VRAIGRLSSM AMISGMSGRK ASGSSPTSPI NADKVENEDA FLEEVAEEKP HVKPYFTKTI
LDMEVVEGSA ARFDCKIEGY PDPEVMWYKD DQPVKESRHF QIDYDEEGNC SLTISEVCGD
DDAKYTCKAV NSLGEATCTA ELLVETMGKE GEGEGEGEED EEEEEE


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U1106h CLIA Homo sapiens,Human,Kinase-related protein,KRP,MLCK,MLCK,MYLK,Myosin light chain kinase, smooth muscle,Telokin 96T
E1106b ELISA kit Bos taurus,Bovine,MLCK,MYLK,Myosin light chain kinase, smooth muscle,Telokin 96T
E1106b ELISA Bos taurus,Bovine,MLCK,MYLK,Myosin light chain kinase, smooth muscle,Telokin 96T
U1106b CLIA Bos taurus,Bovine,MLCK,MYLK,Myosin light chain kinase, smooth muscle,Telokin 96T
U1106m CLIA Kinase-related protein,KRP,MLCK,Mouse,Mus musculus,Mylk,Myosin light chain kinase, smooth muscle,Telokin 96T
E1106m ELISA kit Kinase-related protein,KRP,MLCK,Mouse,Mus musculus,Mylk,Myosin light chain kinase, smooth muscle,Telokin 96T
E1106m ELISA Kinase-related protein,KRP,MLCK,Mouse,Mus musculus,Mylk,Myosin light chain kinase, smooth muscle,Telokin 96T
E1106Rb ELISA MLCK,MYLK,Myosin light chain kinase, smooth muscle,Oryctolagus cuniculus,Rabbit,Telokin 96T
E1106Rb ELISA kit MLCK,MYLK,Myosin light chain kinase, smooth muscle,Oryctolagus cuniculus,Rabbit,Telokin 96T
U1106Rb CLIA MLCK,MYLK,Myosin light chain kinase, smooth muscle,Oryctolagus cuniculus,Rabbit,Telokin 96T
EIAAB26010 17 kDa myosin light chain,Homo sapiens,Human,LC17,MLC-3,MYL6,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Smooth muscle and nonmuscle myosin light
EIAAB26011 17 kDa myosin light chain,LC17,MLC-3,Mouse,Mus musculus,Myl6,Myln,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Smooth muscle and nonmuscle myosin l
EIAAB26007 17 kDa myosin light chain,LC17,MLC-3,Myl6,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Rat,Rattus norvegicus,Smooth muscle and nonmuscle myosin lig
E1106p ELISA MLCK,MYLK,Myosin light chain kinase, smooth muscle,Pig,Sus scrofa 96T
U1106p CLIA MLCK,MYLK,Myosin light chain kinase, smooth muscle,Pig,Sus scrofa 96T
E1106p ELISA kit MLCK,MYLK,Myosin light chain kinase, smooth muscle,Pig,Sus scrofa 96T
EIAAB26013 Homo sapiens,Human,MLC1sa,MLC1SA,MYL6B,Myosin light chain 1 slow-twitch muscle A isoform,Myosin light chain 6B,Smooth muscle and nonmuscle myosin light chain alkali 6B
EIAAB26006 17 kDa myosin light chain,LC17,MLC-3,MYL6,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Pig,Smooth muscle and nonmuscle myosin light chain alkali 6,
EIAAB24918 MLC-2,MLC20,Mrlc2,Mrlcb,Myl12b,Mylc2b,Myosin regulatory light chain 12B,Myosin regulatory light chain 20 kDa,Myosin regulatory light chain 2-B, smooth muscle isoform,Myosin regulatory light chain MRLC
EIAAB24920 Homo sapiens,Human,MLC-2,MLC20,MLC-2A,MRLC2,MYL12B,MYLC2B,Myosin regulatory light chain 12B,Myosin regulatory light chain 20 kDa,Myosin regulatory light chain 2-B, smooth muscle isoform,Myosin regulat
EIAAB24917 Bos taurus,Bovine,MLC20,MRLC2,MYL12B,MYLC2B,Myosin regulatory light chain 12B,Myosin regulatory light chain 20 kDa,Myosin regulatory light chain 2-B, smooth muscle isoform,Myosin regulatory light chai
EIAAB26014 20 kDa myosin light chain,Homo sapiens,Human,LC20,MLC2,MLC-2C,MRLC1,MYL9,Myosin regulatory light chain 2, smooth muscle isoform,Myosin regulatory light chain 9,Myosin regulatory light chain MRLC1,Myos
EIAAB26017 20 kDa myosin light chain,LC20,MYL9,Myosin regulatory light chain 2, smooth muscle isoform,Myosin regulatory light chain 9,Myosin regulatory light polypeptide 9,MYRL2,Pig,Sus scrofa


 

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