Q15746 (MYLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myosin light chain kinase, smooth muscle
Short name=MLCK
Short name=smMLCK
EC=2.7.11.18

Alternative name(s):
Kinase-related protein
Short name=KRP
Telokin

Cleaved into the following chain:

1. Myosin light chain kinase, smooth muscle, deglutamylated form

Gene names

Name:	MYLK
Synonyms:	MLCK, MLCK1, MYLK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1914 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis. Ref.4 Ref.7 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26 Ref.27 Ref.28 Ref.31 Ref.32
Catalytic activity	ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.
Cofactor	Magnesium. Calcium.
Enzyme regulation	Isoform 1 is activated by phosphorylation on Tyr-464 and Tyr-471. Isoforms which lack these tyrosine residues are not regulated in this way. All catalytically active isoforms require binding to calcium and calmodulin for activation. Repressed by organometallic pyridylnaphthalimide complexes, wortmannin, ML-7 (a synthetic naphthalenesulphonyl derivative that inhibits the binding of ATP to MLCK) and ML-9. Ref.4 Ref.15 Ref.16 Ref.19 Ref.20 Ref.33
Subunit structure	All isoforms including Telokin bind calmodulin. Interacts with SVIL By similarity. 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 and PTK2B/PYK2. Ref.14 Ref.23 Ref.26 Ref.29 Ref.30
Subcellular location	Cytoplasm. Cell projection › lamellipodium. Cleavage furrow. Cytoplasm › cytoskeleton. Note: Localized to stress fibers during interphase and to the cleavage furrow during mitosis. Ref.7 Ref.29
Tissue specificity	Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. Telokin has been found in a wide variety of adult and fetal tissues. Accumulates in well differentiated enterocytes of the intestinal epithelium in response to tumor necrosis factor (TNF). Ref.1 Ref.5 Ref.18 Ref.29
Induction	Accumulates in individuals with asthma (at protein levels). Induced by tumor necrosis factor (TNF). Repressed by androgens (e.g. R1881). Ref.4 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.25 Ref.33 Ref.34
Post-translational modification	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-464 and Tyr-471 promotes CTTN binding. 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 By similarity. Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.
Involvement in disease	Familial aortic aneurysm thoracic 7 (AAT7) [MIM:613780]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38
Miscellaneous	In asthmatic patients, overexpression promotes actin filament propulsion, thus contributing to airway hyperresponsiveness. Some MYLK variants may contribute to acute lung injury (ALI) susceptibility. Potential therapeutic target in the treatment of burn edema.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 fibronectin type-III domain. Contains 9 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.
Biophysicochemical properties	Kinetic parameters: KM=6.5 µM for MLC (isoform 1 at 22 degrees Celsius) Ref.4 KM=7.2 µM for MLC (isoform 2 at 22 degrees Celsius) Vmax=11.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius) Vmax=10.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)
Sequence caution	The sequence AAD15922.1 differs from that shown. Reason: Frameshift at position 1433. The sequence AAD15923.1 differs from that shown. Reason: Frameshift at position 1433. The sequence AAD15924.1 differs from that shown. Reason: Frameshift at position 1433. Isoform 3A: The sequence AAD15922.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439. Isoform 3B: The sequence AAD15923.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439. Isoform 4: The sequence AAD15924.1 differs from that shown. Reason: Frameshift at positions 1433 and 1439.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Aortic aneurysm Disease mutation
Domain	Immunoglobulin domain Repeat
Ligand	ATP-binding Actin-binding Calcium Calmodulin-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aorta smooth muscle tissue morphogenesis Inferred from mutant phenotype Ref.38. Source: BHF-UCL bleb assembly Inferred from mutant phenotype Ref.31. Source: UniProtKB cellular hypotonic response Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of calcium ion transport Inferred from direct assay Ref.20. Source: UniProtKB positive regulation of cell migration Inferred from direct assay Ref.26. Source: UniProtKB positive regulation of wound healing Inferred from direct assay Ref.17. Source: UniProtKB tonic smooth muscle contraction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cleavage furrow Inferred from direct assay Ref.7. Source: UniProtKB cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from direct assay Ref.29. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA stress fiber Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin light chain kinase activity Inferred from direct assay Ref.20. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-968482,EBI-389883

Alternative products

This entry describes 8 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q15746-1)

Also known as: Non-muscle isozyme;

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: Q15746-2)

The sequence of this isoform differs from the canonical sequence as follows:
     437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G

Isoform 3A (identifier: Q15746-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1655-1705: Missing.

Isoform 3B (identifier: Q15746-4)

The sequence of this isoform differs from the canonical sequence as follows:
     437-506: VSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVER → G
     1655-1705: Missing.

Isoform 4 (identifier: Q15746-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1473-1545: Missing.

Isoform Del-1790 (identifier: Q15746-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1790-1790: Missing.

Isoform 5 (identifier: Q15746-7)

Also known as: Smooth-muscle isozyme;

The sequence of this isoform differs from the canonical sequence as follows:
     1-922: Missing.

Note: Produced by alternative initiation at Met-923 of isoform 1.

Isoform 6 (identifier: Q15746-8)

Also known as: Telokin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1760: Missing.

Note: Produced by alternative initiation at Met-1761 of isoform 1. Has no catalytic activity.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1914

1914

Myosin light chain kinase, smooth muscle

PRO_0000024354

Chain

1 – 1910

1910

Myosin light chain kinase, smooth muscle, deglutamylated form By similarity

PRO_0000403731

Regions

Domain

33 – 122

90

Ig-like C2-type 1

Domain

161 – 249

89

Ig-like C2-type 2

Domain

414 – 503

90

Ig-like C2-type 3

Domain

514 – 599

86

Ig-like C2-type 4

Domain

620 – 711

92

Ig-like C2-type 5

Domain

721 – 821

101

Ig-like C2-type 6

Repeat

868 – 895

28

1-1

Repeat

896 – 923

28

1-2

Repeat

924 – 951

28

1-3

Repeat

952 – 979

28

1-4

Repeat

980 – 998

19

1-5; truncated

Repeat

999 – 1003

5

2-1; truncated

Repeat

1004 – 1015

12

2-2

Repeat

1016 – 1027

12

2-3

Repeat

1028 – 1039

12

2-4

Repeat

1040 – 1051

12

2-5

Repeat

1052 – 1063

12

2-6

Domain

1098 – 1186

89

Ig-like C2-type 7

Domain

1238 – 1326

89

Ig-like C2-type 8

Domain

1331 – 1422

92

Fibronectin type-III

Domain

1464 – 1719

256

Protein kinase

Domain

1809 – 1898

90

Ig-like C2-type 9

Nucleotide binding

1470 – 1478

9

ATP By similarity

Region

868 – 998

131

5 X 28 AA approximate tandem repeats

Region

923 – 963

41

Actin-binding (calcium/calmodulin-sensitive) By similarity

Region

948 – 963

16

Calmodulin-binding By similarity

Region

999 – 1063

65

6 X 12 AA approximate tandem repeats

Region

1061 – 1460

400

Actin-binding (calcium/calmodulin-insensitive) By similarity

Region

1711 – 1774

64

Calmodulin-binding

Compositional bias

1906 – 1914

9

Poly-Glu

Sites

Active site

1585

1

Proton acceptor By similarity

Binding site

1493

1

ATP By similarity

Amino acid modifications

Modified residue

231

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

343

1

Phosphoserine By similarity

Modified residue

464

1

Phosphotyrosine; by ABL1 and SRC Ref.4 Ref.14 Ref.30

Modified residue

471

1

Phosphotyrosine; by SRC Ref.4 Ref.14

Modified residue

556

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

608

1

N6-acetyllysine Ref.26

Modified residue

611

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

792

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

814

1

Phosphoserine By similarity

Modified residue

846

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

1438

1

Phosphoserine Ref.22 Ref.24

Modified residue

1449

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

1575

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

1635

1

Phosphotyrosine; by ABL1 Ref.30

Modified residue

1759

1

Phosphoserine By similarity

Modified residue

1776

1

Phosphoserine By similarity

Disulfide bond

182 ↔ 233

By similarity

Disulfide bond

435 ↔ 487

By similarity

Disulfide bond

535 ↔ 583

By similarity

Disulfide bond

742 ↔ 805

By similarity

Disulfide bond

1119 ↔ 1170

By similarity

Disulfide bond

1830 ↔ 1882

By similarity

Natural variations

Alternative sequence

1 – 1760

1760

Missing in isoform 6.

VSP_018846

Alternative sequence

1 – 922

922

Missing in isoform 5.

VSP_018845

Alternative sequence

437 – 506

70

VSGIP…LQVER → G in isoform 2 and isoform 3B.

VSP_004791

Alternative sequence

1473 – 1545

73

Missing in isoform 4.

VSP_004793

Alternative sequence

1655 – 1705

51

Missing in isoform 3A and isoform 3B.

VSP_004794

Alternative sequence

1790

1

Missing in isoform Del-1790.

VSP_004795

Natural variant

21

1

P → H.
Corresponds to variant rs28497577 [ dbSNP | Ensembl ].

VAR_057106

Natural variant

128

1

A → V. Ref.38

VAR_065570

Natural variant

133

1

Q → H. Ref.38

VAR_065571

Natural variant

160

1

P → R. Ref.38

VAR_065572

Natural variant

261

1

V → A. Ref.37
Corresponds to variant rs3796164 [ dbSNP | Ensembl ].

VAR_040847

Natural variant

276

1

T → A. Ref.37

VAR_040848

Natural variant

336

1

P → L.
Corresponds to variant rs35912339 [ dbSNP | Ensembl ].

VAR_057107

Natural variant

378

1

R → H. Ref.37

VAR_040849

Natural variant

405

1

M → V. Ref.37
Corresponds to variant rs35436690 [ dbSNP | Ensembl ].

VAR_040850

Natural variant

443

1

P → S. Ref.37

VAR_040851

Natural variant

607

1

R → G. Ref.37

VAR_040852

Natural variant

652

1

P → A. Ref.37

VAR_040853

Natural variant

656

1

W → C. Ref.37 Ref.38

VAR_040854

Natural variant

692

1

T → M. Ref.37

VAR_040855

Natural variant

701

1

A → T. Ref.37

VAR_040856

Natural variant

709

1

V → M. Ref.37

VAR_040857

Natural variant

845

1

R → C.
Corresponds to variant rs3732485 [ dbSNP | Ensembl ].

VAR_057108

Natural variant

861

1

L → P.
Corresponds to variant rs3732486 [ dbSNP | Ensembl ].

VAR_019986

Natural variant

877

1

V → M.
Corresponds to variant rs34542174 [ dbSNP | Ensembl ].

VAR_057109

Natural variant

914

1

D → E.
Corresponds to variant rs3732487 [ dbSNP | Ensembl ].

VAR_019987

Natural variant

1085

1

T → A. Ref.38

VAR_065573

Natural variant

1213

1

V → M Found in a patient with familial aortic dissections. Ref.38

VAR_065574

Natural variant

1399

1

E → K Found in a patient with familial aortic dissections. Ref.38

VAR_065575

Natural variant

1527

1

A → V. Ref.37

VAR_040858

Natural variant

1588

1

P → L in an ovarian mucinous carcinoma sample; somatic mutation. Ref.37

VAR_040859

Natural variant

1754

1

A → T Found in a patient with familial aortic dissections; binding to calmodulin is reduced; significant reduction in kinase activity compared to wild-type protein. Ref.38

VAR_065576

Natural variant

1759

1

S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. Ref.38

VAR_065577

Experimental info

Mutagenesis

608

1

K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. Ref.26

Sequence conflict

147

1

P → S in AAC18423. Ref.2

Sequence conflict

147

1

P → S in AAD15922. Ref.3

Sequence conflict

147

1

P → S in AAD15923. Ref.3

Sequence conflict

147

1

P → S in AAR29062. Ref.6

Sequence conflict

147

1

P → S in AAQ02673. Ref.7

Sequence conflict

466

1

D → N in AAR29062. Ref.6

Sequence conflict

496

1

L → V in AAC18423. Ref.2

Sequence conflict

496

1

L → V in AAD15922. Ref.3

Sequence conflict

496

1

L → V in AAR29062. Ref.6

Sequence conflict

496

1

L → V in AAQ02673. Ref.7

Sequence conflict

681

1

C → W in AAC18423. Ref.2

Sequence conflict

681

1

C → W in AAD15921. Ref.3

Sequence conflict

681

1

C → W in AAD15922. Ref.3

Sequence conflict

681

1

C → W in AAD15923. Ref.3

Sequence conflict

933

1

V → M in CAA59685. Ref.1

Sequence conflict

963

1

S → P in AAD15922. Ref.3

Sequence conflict

1022

1

P → A in CAA59685. Ref.1

Sequence conflict

1048 – 1050

3

KPM → EAH Ref.1

Sequence conflict

1048 – 1050

3

KPM → EAH Ref.8

Sequence conflict

1162

1

P → L in AAD15922. Ref.3

Sequence conflict

1162

1

P → L in AAD15923. Ref.3

Sequence conflict

1210

1

L → P in CAA59685. Ref.1

Sequence conflict

1280

1

E → D in AAD15922. Ref.3

Sequence conflict

1280

1

E → D in AAD15923. Ref.3

Sequence conflict

1284

1

M → I in AAD15922. Ref.3

Sequence conflict

1284

1

M → I in AAD15923. Ref.3

Sequence conflict

1284

1

M → I in AAD15924. Ref.3

Sequence conflict

1300

1

A → G in CAA59685. Ref.1

Sequence conflict

1316

1

L → S in CAA59685. Ref.1

Sequence conflict

1326

1

T → S in CAA59685. Ref.1

Sequence conflict

1478

1

V → C in CAA59685. Ref.1

Sequence conflict

1511

1

S → T in AAD15922. Ref.3

Sequence conflict

1511

1

S → T in AAD15923. Ref.3

Sequence conflict

1518

1

H → P in AAR29061. Ref.6

Sequence conflict

1518

1

H → P in AAR29062. Ref.6

Sequence conflict

1563

1

I → T in CAA59685. Ref.1

Sequence conflict

1609

1

A → P in CAA59685. Ref.1

Sequence conflict

1634

1

N → I in AAR29061. Ref.6

Sequence conflict

1634

1

N → I in AAR29062. Ref.6

Sequence conflict

1639 – 1640

2

GY → D in AAD15922. Ref.3

Sequence conflict

1639 – 1640

2

GY → D in AAD15923. Ref.3

Sequence conflict

1639 – 1640

2

GY → D in AAD15924. Ref.3

Sequence conflict

1639

1

G → R in CAA59685. Ref.1

Sequence conflict

1648

1

G → R in CAA59685. Ref.1

Sequence conflict

1658 – 1659

2

LS → PF in CAA59685. Ref.1

Sequence conflict

1676

1

A → P in AAR29061. Ref.6

Sequence conflict

1676

1

A → P in AAR29062. Ref.6

Sequence conflict

1710 – 1711

2

CT → LA in CAA59685. Ref.1

Sequence conflict

1897

1

L → H in AAD15922. Ref.3

Sequence conflict

1897

1

L → H in AAD15923. Ref.3

Sequence conflict

1897

1

L → H in AAD15924. Ref.3

Secondary structure

1

.

.

.

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.

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1914

Helix Strand Turn

Details...

Beta strand

512 – 518

7

Beta strand

523 – 526

4

Beta strand

531 – 534

4

Beta strand

536 – 541

6

Beta strand

546 – 553

8

Beta strand

560 – 562

3

Beta strand

565 – 570

6

Beta strand

581 – 586

6

Beta strand

591 – 595

5

Beta strand

598 – 601

4

Beta strand

1239 – 1241

3

Beta strand

1246 – 1250

5

Beta strand

1255 – 1266

12

Beta strand

1268 – 1277

10

Beta strand

1281 – 1288

8

Beta strand

1290 – 1297

8

Turn

1302 – 1304

3

Beta strand

1306 – 1313

8

Beta strand

1318 – 1320

3

Beta strand

1323 – 1328

6

Helix

1743 – 1759

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Non-muscle isozyme) [UniParc]. Last modified July 13, 2010. Version 4. Checksum: 2D094E161CE2D4BA	FASTA	1,914	210,715
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLKARTR 490 500 510 520 530 540 DSGTYSCTAS NAQGQLSCSW TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT 550 560 570 580 590 600 PVPRITWLLN GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 610 620 630 640 650 660 HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG 670 680 690 700 710 720 NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ 730 740 750 760 770 780 PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV 790 800 810 820 830 840 LKKVQPWHAG QYEILLKNRV GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG 850 860 870 880 890 900 GGSDRYGSLR PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 910 920 930 940 950 960 LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK 970 980 990 1000 1010 1020 GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS 1030 1040 1050 1060 1070 1080 GPLKPVGNAK PAETLKPMGN AKPAETLKPM GNAKPDENLK SASKEELKKD VKNDVNCKRG 1090 1100 1110 1120 1130 1140 HAGTTDNEKR SESQGTAPAF KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT 1150 1160 1170 1180 1190 1200 TKFIILSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 1210 1220 1230 1240 1250 1260 MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELFGK 1270 1280 1290 1300 1310 1320 VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ 1330 1340 1350 1360 1370 1380 AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE 1390 1400 1410 1420 1430 1440 LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD 1450 1460 1470 1480 1490 1500 DEKEPEVDYR TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA 1510 1520 1530 1540 1550 1560 KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI IDEDFELTER 1570 1580 1590 1600 1610 1620 ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR IKLIDFGLAR RLENAGSLKV 1630 1640 1650 1660 1670 1680 LFGTPEFVAP EVINYEPIGY ATDMWSIGVI CYILVSGLSP FMGDNDNETL ANVTSATWDF 1690 1700 1710 1720 1730 1740 DDEAFDEISD DAKDFISNLL KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM 1750 1760 1770 1780 1790 1800 ARRKWQKTGN AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV 1810 1820 1830 1840 1850 1860 AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD 1870 1880 1890 1900 1910 EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE
	Isoform 2 [UniParc]. Checksum: 0111D4C5A88349AB	FASTA	1,845	203,055
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEGLAV MEVAPSFSSV LKDCAVIEGQ DFVLQCSVRG TPVPRITWLL 490 500 510 520 530 540 NGQPIQYARS TCEAGVAELH IQDALPEDHG TYTCLAENAL GQVSCSAWVT VHEKKSSRKS 550 560 570 580 590 600 EYLLPVAPSK PTAPIFLQGL SDLKVMDGSQ VTMTVQVSGN PPPEVIWLHN GNEIQESEDF 610 620 630 640 650 660 HFEQRGTQHS LCIQEVFPED TGTYTCEAWN SAGEVRTQAV LTVQEPHDGT QPWFISKPRS 670 680 690 700 710 720 VTASLGQSVL ISCAIAGDPF PTVHWLRDGK ALCKDTGHFE VLQNEDVFTL VLKKVQPWHA 730 740 750 760 770 780 GQYEILLKNR VGECSCQVSL MLQNSSARAL PRGREPASCE DLCGGGVGAD GGGSDRYGSL 790 800 810 820 830 840 RPGWPARGQG WLEEEDGEDV RGVLKRRVET RQHTEEAIRQ QEVEQLDFRD LLGKKVSTKT 850 860 870 880 890 900 LSEDDLKEIP AEQMDFRANL QRQVKPKTVS EEERKVHSPQ QVDFRSVLAK KGTSKTPVPE 910 920 930 940 950 960 KVPPPKPATP DFRSVLGGKK KLPAENGSSS AETLNAKAVE SSKPLSNAQP SGPLKPVGNA 970 980 990 1000 1010 1020 KPAETLKPMG NAKPAETLKP MGNAKPDENL KSASKEELKK DVKNDVNCKR GHAGTTDNEK 1030 1040 1050 1060 1070 1080 RSESQGTAPA FKQKLQDVHV AEGKKLLLQC QVSSDPPATI IWTLNGKTLK TTKFIILSQE 1090 1100 1110 1120 1130 1140 GSLCSVSIEK ALPEDRGLYK CVAKNDAGQA ECSCQVTVDD APASENTKAP EMKSRRPKSS 1150 1160 1170 1180 1190 1200 LPPVLGTESD ATVKKKPAPK TPPKAAMPPQ IIQFPEDQKV RAGESVELFG KVTGTQPITC 1210 1220 1230 1240 1250 1260 TWMKFRKQIQ ESEHMKVENS ENGSKLTILA ARQEHCGCYT LLVENKLGSR QAQVNLTVVD 1270 1280 1290 1300 1310 1320 KPDPPAGTPC ASDIRSSSLT LSWYGSSYDG GSAVQSYSIE IWDSANKTWK ELATCRSTSF 1330 1340 1350 1360 1370 1380 NVQDLLPDHE YKFRVRAINV YGTSEPSQES ELTTVGEKPE EPKDEVEVSD DDEKEPEVDY 1390 1400 1410 1420 1430 1440 RTVTINTEQK VSDFYDIEER LGSGKFGQVF RLVEKKTRKV WAGKFFKAYS AKEKENIRQE 1450 1460 1470 1480 1490 1500 ISIMNCLHHP KLVQCVDAFE EKANIVMVLE IVSGGELFER IIDEDFELTE RECIKYMRQI 1510 1520 1530 1540 1550 1560 SEGVEYIHKQ GIVHLDLKPE NIMCVNKTGT RIKLIDFGLA RRLENAGSLK VLFGTPEFVA 1570 1580 1590 1600 1610 1620 PEVINYEPIG YATDMWSIGV ICYILVSGLS PFMGDNDNET LANVTSATWD FDDEAFDEIS 1630 1640 1650 1660 1670 1680 DDAKDFISNL LKKDMKNRLD CTQCLQHPWL MKDTKNMEAK KLSKDRMKKY MARRKWQKTG 1690 1700 1710 1720 1730 1740 NAVRAIGRLS SMAMISGLSG RKSSTGSPTS PLNAEKLESE EDVSQAFLEA VAEEKPHVKP 1750 1760 1770 1780 1790 1800 YFSKTIRDLE VVEGSAARFD CKIEGYPDPE VVWFKDDQSI RESRHFQIDY DEDGNCSLII 1810 1820 1830 1840 SDVCGDDDAK YTCKAVNSLG EATCTAELIV ETMEEGEGEG EEEEE
	Isoform 3A [UniParc]. Checksum: A526210F1B9E546C	FASTA	1,863	205,059
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLKARTR 490 500 510 520 530 540 DSGTYSCTAS NAQGQLSCSW TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT 550 560 570 580 590 600 PVPRITWLLN GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 610 620 630 640 650 660 HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG 670 680 690 700 710 720 NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ 730 740 750 760 770 780 PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV 790 800 810 820 830 840 LKKVQPWHAG QYEILLKNRV GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG 850 860 870 880 890 900 GGSDRYGSLR PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 910 920 930 940 950 960 LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK 970 980 990 1000 1010 1020 GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS 1030 1040 1050 1060 1070 1080 GPLKPVGNAK PAETLKPMGN AKPAETLKPM GNAKPDENLK SASKEELKKD VKNDVNCKRG 1090 1100 1110 1120 1130 1140 HAGTTDNEKR SESQGTAPAF KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT 1150 1160 1170 1180 1190 1200 TKFIILSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 1210 1220 1230 1240 1250 1260 MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELFGK 1270 1280 1290 1300 1310 1320 VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ 1330 1340 1350 1360 1370 1380 AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE 1390 1400 1410 1420 1430 1440 LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD 1450 1460 1470 1480 1490 1500 DEKEPEVDYR TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA 1510 1520 1530 1540 1550 1560 KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI IDEDFELTER 1570 1580 1590 1600 1610 1620 ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR IKLIDFGLAR RLENAGSLKV 1630 1640 1650 1660 1670 1680 LFGTPEFVAP EVINYEPIGY ATDMWSIGVI CYILNRLDCT QCLQHPWLMK DTKNMEAKKL 1690 1700 1710 1720 1730 1740 SKDRMKKYMA RRKWQKTGNA VRAIGRLSSM AMISGLSGRK SSTGSPTSPL NAEKLESEED 1750 1760 1770 1780 1790 1800 VSQAFLEAVA EEKPHVKPYF SKTIRDLEVV EGSAARFDCK IEGYPDPEVV WFKDDQSIRE 1810 1820 1830 1840 1850 1860 SRHFQIDYDE DGNCSLIISD VCGDDDAKYT CKAVNSLGEA TCTAELIVET MEEGEGEGEE EEE
	Isoform 3B [UniParc]. Checksum: 9EE35F5BADBB0D9A	FASTA	1,794	197,399
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEGLAV MEVAPSFSSV LKDCAVIEGQ DFVLQCSVRG TPVPRITWLL 490 500 510 520 530 540 NGQPIQYARS TCEAGVAELH IQDALPEDHG TYTCLAENAL GQVSCSAWVT VHEKKSSRKS 550 560 570 580 590 600 EYLLPVAPSK PTAPIFLQGL SDLKVMDGSQ VTMTVQVSGN PPPEVIWLHN GNEIQESEDF 610 620 630 640 650 660 HFEQRGTQHS LCIQEVFPED TGTYTCEAWN SAGEVRTQAV LTVQEPHDGT QPWFISKPRS 670 680 690 700 710 720 VTASLGQSVL ISCAIAGDPF PTVHWLRDGK ALCKDTGHFE VLQNEDVFTL VLKKVQPWHA 730 740 750 760 770 780 GQYEILLKNR VGECSCQVSL MLQNSSARAL PRGREPASCE DLCGGGVGAD GGGSDRYGSL 790 800 810 820 830 840 RPGWPARGQG WLEEEDGEDV RGVLKRRVET RQHTEEAIRQ QEVEQLDFRD LLGKKVSTKT 850 860 870 880 890 900 LSEDDLKEIP AEQMDFRANL QRQVKPKTVS EEERKVHSPQ QVDFRSVLAK KGTSKTPVPE 910 920 930 940 950 960 KVPPPKPATP DFRSVLGGKK KLPAENGSSS AETLNAKAVE SSKPLSNAQP SGPLKPVGNA 970 980 990 1000 1010 1020 KPAETLKPMG NAKPAETLKP MGNAKPDENL KSASKEELKK DVKNDVNCKR GHAGTTDNEK 1030 1040 1050 1060 1070 1080 RSESQGTAPA FKQKLQDVHV AEGKKLLLQC QVSSDPPATI IWTLNGKTLK TTKFIILSQE 1090 1100 1110 1120 1130 1140 GSLCSVSIEK ALPEDRGLYK CVAKNDAGQA ECSCQVTVDD APASENTKAP EMKSRRPKSS 1150 1160 1170 1180 1190 1200 LPPVLGTESD ATVKKKPAPK TPPKAAMPPQ IIQFPEDQKV RAGESVELFG KVTGTQPITC 1210 1220 1230 1240 1250 1260 TWMKFRKQIQ ESEHMKVENS ENGSKLTILA ARQEHCGCYT LLVENKLGSR QAQVNLTVVD 1270 1280 1290 1300 1310 1320 KPDPPAGTPC ASDIRSSSLT LSWYGSSYDG GSAVQSYSIE IWDSANKTWK ELATCRSTSF 1330 1340 1350 1360 1370 1380 NVQDLLPDHE YKFRVRAINV YGTSEPSQES ELTTVGEKPE EPKDEVEVSD DDEKEPEVDY 1390 1400 1410 1420 1430 1440 RTVTINTEQK VSDFYDIEER LGSGKFGQVF RLVEKKTRKV WAGKFFKAYS AKEKENIRQE 1450 1460 1470 1480 1490 1500 ISIMNCLHHP KLVQCVDAFE EKANIVMVLE IVSGGELFER IIDEDFELTE RECIKYMRQI 1510 1520 1530 1540 1550 1560 SEGVEYIHKQ GIVHLDLKPE NIMCVNKTGT RIKLIDFGLA RRLENAGSLK VLFGTPEFVA 1570 1580 1590 1600 1610 1620 PEVINYEPIG YATDMWSIGV ICYILNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM 1630 1640 1650 1660 1670 1680 ARRKWQKTGN AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV 1690 1700 1710 1720 1730 1740 AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD 1750 1760 1770 1780 1790 EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE
	Isoform 4 [UniParc]. Checksum: 23EDB48D1A11DE70	FASTA	1,841	202,350
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLKARTR 490 500 510 520 530 540 DSGTYSCTAS NAQGQLSCSW TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT 550 560 570 580 590 600 PVPRITWLLN GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 610 620 630 640 650 660 HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG 670 680 690 700 710 720 NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ 730 740 750 760 770 780 PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV 790 800 810 820 830 840 LKKVQPWHAG QYEILLKNRV GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG 850 860 870 880 890 900 GGSDRYGSLR PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 910 920 930 940 950 960 LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK 970 980 990 1000 1010 1020 GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS 1030 1040 1050 1060 1070 1080 GPLKPVGNAK PAETLKPMGN AKPAETLKPM GNAKPDENLK SASKEELKKD VKNDVNCKRG 1090 1100 1110 1120 1130 1140 HAGTTDNEKR SESQGTAPAF KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT 1150 1160 1170 1180 1190 1200 TKFIILSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 1210 1220 1230 1240 1250 1260 MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELFGK 1270 1280 1290 1300 1310 1320 VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ 1330 1340 1350 1360 1370 1380 AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE 1390 1400 1410 1420 1430 1440 LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD 1450 1460 1470 1480 1490 1500 DEKEPEVDYR TVTINTEQKV SDFYDIEERL GSLFERIIDE DFELTERECI KYMRQISEGV 1510 1520 1530 1540 1550 1560 EYIHKQGIVH LDLKPENIMC VNKTGTRIKL IDFGLARRLE NAGSLKVLFG TPEFVAPEVI 1570 1580 1590 1600 1610 1620 NYEPIGYATD MWSIGVICYI LVSGLSPFMG DNDNETLANV TSATWDFDDE AFDEISDDAK 1630 1640 1650 1660 1670 1680 DFISNLLKKD MKNRLDCTQC LQHPWLMKDT KNMEAKKLSK DRMKKYMARR KWQKTGNAVR 1690 1700 1710 1720 1730 1740 AIGRLSSMAM ISGLSGRKSS TGSPTSPLNA EKLESEEDVS QAFLEAVAEE KPHVKPYFSK 1750 1760 1770 1780 1790 1800 TIRDLEVVEG SAARFDCKIE GYPDPEVVWF KDDQSIRESR HFQIDYDEDG NCSLIISDVC 1810 1820 1830 1840 GDDDAKYTCK AVNSLGEATC TAELIVETME EGEGEGEEEE E
	Isoform Del-1790 [UniParc]. Checksum: 6D3029D5CCA13B41	FASTA	1,913	210,586
	10 20 30 40 50 60 MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP 70 80 90 100 110 120 EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE 130 140 150 160 170 180 LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF 190 200 210 220 230 240 SCKITGRPQP QVTWLKGNVP LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG 250 260 270 280 290 300 KASMSAELSI QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP 310 320 330 340 350 360 QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA RVQPEPRAPG 370 380 390 400 410 420 LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN RRIPMEGQRD SAFPKFESKP 430 440 450 460 470 480 QSQEVKENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLKARTR 490 500 510 520 530 540 DSGTYSCTAS NAQGQLSCSW TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT 550 560 570 580 590 600 PVPRITWLLN GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV 610 620 630 640 650 660 HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG 670 680 690 700 710 720 NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ 730 740 750 760 770 780 PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV 790 800 810 820 830 840 LKKVQPWHAG QYEILLKNRV GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG 850 860 870 880 890 900 GGSDRYGSLR PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL 910 920 930 940 950 960 LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK 970 980 990 1000 1010 1020 GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS 1030 1040 1050 1060 1070 1080 GPLKPVGNAK PAETLKPMGN AKPAETLKPM GNAKPDENLK SASKEELKKD VKNDVNCKRG 1090 1100 1110 1120 1130 1140 HAGTTDNEKR SESQGTAPAF KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT 1150 1160 1170 1180 1190 1200 TKFIILSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE 1210 1220 1230 1240 1250 1260 MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELFGK 1270 1280 1290 1300 1310 1320 VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ 1330 1340 1350 1360 1370 1380 AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE 1390 1400 1410 1420 1430 1440 LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD 1450 1460 1470 1480 1490 1500 DEKEPEVDYR TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA 1510 1520 1530 1540 1550 1560 KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI IDEDFELTER 1570 1580 1590 1600 1610 1620 ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR IKLIDFGLAR RLENAGSLKV 1630 1640 1650 1660 1670 1680 LFGTPEFVAP EVINYEPIGY ATDMWSIGVI CYILVSGLSP FMGDNDNETL ANVTSATWDF 1690 1700 1710 1720 1730 1740 DDEAFDEISD DAKDFISNLL KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM 1750 1760 1770 1780 1790 1800 ARRKWQKTGN AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESED VSQAFLEAVA 1810 1820 1830 1840 1850 1860 EEKPHVKPYF SKTIRDLEVV EGSAARFDCK IEGYPDPEVV WFKDDQSIRE SRHFQIDYDE 1870 1880 1890 1900 1910 DGNCSLIISD VCGDDDAKYT CKAVNSLGEA TCTAELIVET MEEGEGEGEE EEE
	Isoform 5 (Smooth-muscle isozyme) [UniParc]. Checksum: 27288359F94FE260	FASTA	992	110,205
	10 20 30 40 50 60 MDFRANLQRQ VKPKTVSEEE RKVHSPQQVD FRSVLAKKGT SKTPVPEKVP PPKPATPDFR 70 80 90 100 110 120 SVLGGKKKLP AENGSSSAET LNAKAVESSK PLSNAQPSGP LKPVGNAKPA ETLKPMGNAK 130 140 150 160 170 180 PAETLKPMGN AKPDENLKSA SKEELKKDVK NDVNCKRGHA GTTDNEKRSE SQGTAPAFKQ 190 200 210 220 230 240 KLQDVHVAEG KKLLLQCQVS SDPPATIIWT LNGKTLKTTK FIILSQEGSL CSVSIEKALP 250 260 270 280 290 300 EDRGLYKCVA KNDAGQAECS CQVTVDDAPA SENTKAPEMK SRRPKSSLPP VLGTESDATV 310 320 330 340 350 360 KKKPAPKTPP KAAMPPQIIQ FPEDQKVRAG ESVELFGKVT GTQPITCTWM KFRKQIQESE 370 380 390 400 410 420 HMKVENSENG SKLTILAARQ EHCGCYTLLV ENKLGSRQAQ VNLTVVDKPD PPAGTPCASD 430 440 450 460 470 480 IRSSSLTLSW YGSSYDGGSA VQSYSIEIWD SANKTWKELA TCRSTSFNVQ DLLPDHEYKF 490 500 510 520 530 540 RVRAINVYGT SEPSQESELT TVGEKPEEPK DEVEVSDDDE KEPEVDYRTV TINTEQKVSD 550 560 570 580 590 600 FYDIEERLGS GKFGQVFRLV EKKTRKVWAG KFFKAYSAKE KENIRQEISI MNCLHHPKLV 610 620 630 640 650 660 QCVDAFEEKA NIVMVLEIVS GGELFERIID EDFELTEREC IKYMRQISEG VEYIHKQGIV 670 680 690 700 710 720 HLDLKPENIM CVNKTGTRIK LIDFGLARRL ENAGSLKVLF GTPEFVAPEV INYEPIGYAT 730 740 750 760 770 780 DMWSIGVICY ILVSGLSPFM GDNDNETLAN VTSATWDFDD EAFDEISDDA KDFISNLLKK 790 800 810 820 830 840 DMKNRLDCTQ CLQHPWLMKD TKNMEAKKLS KDRMKKYMAR RKWQKTGNAV RAIGRLSSMA 850 860 870 880 890 900 MISGLSGRKS STGSPTSPLN AEKLESEEDV SQAFLEAVAE EKPHVKPYFS KTIRDLEVVE 910 920 930 940 950 960 GSAARFDCKI EGYPDPEVVW FKDDQSIRES RHFQIDYDED GNCSLIISDV CGDDDAKYTC 970 980 990 KAVNSLGEAT CTAELIVETM EEGEGEGEEE EE
	Isoform 6 (Telokin) [UniParc]. Checksum: 0E3B6CAD36C563EE	FASTA	154	16,970
	10 20 30 40 50 60 MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV AEEKPHVKPY FSKTIRDLEV 70 80 90 100 110 120 VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY 130 140 150 TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE

References

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[1]	"The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21." Potier M.-C., Chelot E., Pekarsky Y., Gardiner K., Rossier J., Turnell W.G. Genomics 29:562-570(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY. Tissue: Hippocampus.
[2]	"Myosin light chain kinase in endothelium: molecular cloning and regulation." Garcia J.G.N., Lazar V.L., Gilbert-Mcclain L.I., Gallagher P.J., Verin A.D. Am. J. Respir. Cell Mol. Biol. 16:489-494(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Umbilical vein endothelial cell.
[3]	"A single human myosin light chain kinase gene (MLCK; MYLK)." Lazar V.L., Garcia J.G.N. Genomics 57:256-267(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3A; 3B AND 4). Tissue: Umbilical vein.
[4]	"Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src)." Birukov K.G., Csortos C., Marzilli L., Dudek S., Ma S.-F., Bresnick A.R., Verin A.D., Cotter R.J., Garcia J.G.N. J. Biol. Chem. 276:8567-8573(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 457-476 AND 968-985, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT TYR-464 AND TYR-471, CALMODULIN-BINDING, ENZYME REGULATION.
[5]	"Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing and polymorphic marker." Watterson D.M., Schavocky J.P., Guo L., Weiss C., Chlenski A., Shrinsky V.P., Van Eldik L.J., Haiech J. J. Cell. Biochem. 75:481-491(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1614-1914 (ISOFORM 5), TISSUE SPECIFICITY. Tissue: Lung and Placenta.
[6]	"A differentiation-dependent splice variant of myosin light chain kinase, MLCK1, regulates epithelial tight junction permeability." Clayburgh D.R., Rosen S., Witkowski E.D., Wang F., Blair S., Dudek S., Garcia J.G., Alverdy J.C., Turner J.R. J. Biol. Chem. 279:55506-55513(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Intestinal epithelium.
[7]	"The N-terminus of the long MLCK induces a disruption in normal spindle morphology and metaphase arrest." Dulyaninova N.G., Patskovsky Y.V., Bresnick A.R. J. Cell Sci. 117:1481-1493(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CELL CYCLE, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[8]	"HeLa myosin light chain kinase." Kikuchi A., Murata-Hori M., Hosoya H. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Cervix carcinoma.
[9]	"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. , 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 6). Tissue: Testis.
[10]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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 6).
[13]	Watterson D.M. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1456-1914. Tissue: Placenta.
[14]	"Novel interaction of cortactin with endothelial cell myosin light chain kinase." Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N. Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTTN, PHOSPHORYLATION AT TYR-464 AND TYR-471 BY SRC.
[15]	"Myosin light chain kinase modulates hypotonicity-induced Ca2+ entry and Cl- channel activity in human cervical cancer cells." Shen M.-R., Furla P., Chou C.-Y., Ellory J.C. Pflugers Arch. 444:276-285(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HYPOTONICITY RESPONSE, ENZYME REGULATION.
[16]	"Quantitative measurements of Ca(2+)/calmodulin binding and activation of myosin light chain kinase in cells." Geguchadze R., Zhi G., Lau K.S., Isotani E., Persechini A., Kamm K.E., Stull J.T. FEBS Lett. 557:121-124(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION BY CALCIUM.
[17]	"Distinct temporal-spatial roles for rho kinase and myosin light chain kinase in epithelial purse-string wound closure." Russo J.M., Florian P., Shen L., Graham W.V., Tretiakova M.S., Gitter A.H., Mrsny R.J., Turner J.R. Gastroenterology 128:987-1001(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN WOUND HEALING.
[18]	"Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter." Graham W.V., Wang F., Clayburgh D.R., Cheng J.X., Yoon B., Wang Y., Lin A., Turner J.R. J. Biol. Chem. 281:26205-26215(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY TNF, TISSUE SPECIFICITY.
[19]	"Myosin light chain kinase plays a role in the regulation of epithelial cell survival." Connell L.E., Helfman D.M. J. Cell Sci. 119:2269-2281(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EPITHELIAL CELL SURVIVAL, ENZYME REGULATION.
[20]	"Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells." Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y. J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRPC5 REGULATION, ENZYME REGULATION.
[21]	"Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2." Zhou X., Liu Y., You J., Zhang H., Zhang X., Ye L. Cancer Lett. 270:312-327(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL MIGRATION.
[22]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, MASS SPECTROMETRY. Tissue: Platelet.
[23]	"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.
[24]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, MASS SPECTROMETRY. Tissue: Liver.
[25]	"Androgens down-regulate myosin light chain kinase in human prostate cancer cells." Leveille N., Fournier A., Labrie C. J. Steroid Biochem. Mol. Biol. 114:174-179(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY ANDROGENS.
[26]	"Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase." Shin D.H., Chun Y.-S., Lee K.-H., Shin H.-W., Park J.-W. PLoS ONE 4:E7451-E7451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TUMOR CELL MIGRATION, ACETYLATION AT LYS-608 BY NAA10/ARD1, INTERACTION WITH NAA10/ARD1, MUTAGENESIS OF LYS-608.
[27]	"Myosin light chain kinase is responsible for high proliferative ability of breast cancer cells via anti-apoptosis involving p38 pathway." Cui W.-J., Liu Y., Zhou X.-L., Wang F.-Z., Zhang X.-D., Ye L.-H. Acta Pharmacol. Sin. 31:725-732(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN BREAST CANCER.
[28]	"Modulation of factors affecting optic nerve head astrocyte migration." Miao H., Crabb A.W., Hernandez M.R., Lukas T.J. Invest. Ophthalmol. Vis. Sci. 51:4096-4103(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN OPTIC NERVE HEAD ASTROCYTE MIGRATION.
[29]	"Quantitative distribution and colocalization of non-muscle myosin light chain kinase isoforms and cortactin in human lung endothelium." Brown M., Adyshev D., Bindokas V., Moitra J., Garcia J.G.N., Dudek S.M. Microvasc. Res. 80:75-88(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH CTTN, SUBCELLULAR LOCATION.
[30]	"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function." Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N. Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-231; TYR-464; TYR-556; TYR-611; TYR-792; TYR-846; TYR-1449; TYR-1575 AND TYR-1635 BY ABL1, INTERACTION WITH CTTN AND ABL1.
[31]	"The angiotensin II type 1 receptor induces membrane blebbing by coupling to Rho A, Rho kinase, and myosin light chain kinase." Godin C.M., Ferguson S.S.G. Mol. Pharmacol. 77:903-911(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MEMBRANE BLEBBING.
[32]	"Non-muscle myosin light chain kinase isoform is a viable molecular target in acute inflammatory lung injury." Mirzapoiazova T., Moitra J., Moreno-Vinasco L., Sammani S., Turner J.R., Chiang E.T., Evenoski C., Wang T., Singleton P.A., Huang Y., Lussier Y.A., Watterson D.M., Dudek S.M., Garcia J.G.N. Am. J. Respir. Cell Mol. Biol. 44:40-52(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
[33]	"Organometallic pyridylnaphthalimide complexes as protein kinase inhibitors." Blanck S., Cruchter T., Vultur A., Riedel R., Harms K., Herlyn M., Meggers E. Organometallics 30:4598-4606(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[34]	"Myosin, transgelin, and myosin light chain kinase: expression and function in asthma." Leguillette R., Laviolette M., Bergeron C., Zitouni N., Kogut P., Solway J., Kachmar L., Hamid Q., Lauzon A.-M. Am. J. Respir. Crit. Care Med. 179:194-204(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ASTHMA, INDUCTION BY ASTHMA.
[35]	"Solution structure of the eighth Ig-like domain of human myosin light chain kinase." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1238-1338.
[36]	"A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction." Gsponer J., Christodoulou J., Cavalli A., Bui J.M., Richter B., Dobson C.M., Vendruscolo M. Structure 16:736-746(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1742-1760 IN COMPLEX WITH CALMODULIN.
[37]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-261; ALA-276; HIS-378; VAL-405; SER-443; GLY-607; ALA-652; CYS-656; MET-692; THR-701; MET-709; VAL-1527 AND LEU-1588.
[38]	"Mutations in myosin light chain kinase cause familial aortic dissections." Wang L., Guo D.C., Cao J., Gong L., Kamm K.E., Regalado E., Li L., Shete S., He W.Q., Zhu M.S., Offermanns S., Gilchrist D., Elefteriades J., Stull J.T., Milewicz D.M. Am. J. Hum. Genet. 87:701-707(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AAT7 PRO-1759, VARIANTS VAL-128; HIS-133; ARG-160; CYS-656; ALA-1085; MET-1213; LYS-1399 AND THR-1754, CHARACTERIZATION OF VARIANT AAT7 PRO-1759, CHARACTERIZATION OF VARIANT THR-1754.
+	Additional computationally mapped references.

Web resources

Wikipedia

Myosin light-chain kinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X85337 mRNA. Translation: CAA59685.1.
U48959 mRNA. Translation: AAC18423.2.
AF069601 mRNA. Translation: AAD15921.2.
AF069602 mRNA. Translation: AAD15922.1. Frameshift.
AF069603 mRNA. Translation: AAD15923.1. Frameshift.
AF069604 mRNA. Translation: AAD15924.1. Frameshift.
AF096771 , AF096766, AF096767, AF096768, AF096769, AF096770 Genomic DNA. Translation: AAD51380.1.
AF096771, AF096769, AF096770 Genomic DNA. Translation: AAD51381.1.
AF096773 mRNA. Translation: AAD54017.1.
AF096774 mRNA. Translation: AAD54018.1.
AF096775 mRNA. Translation: AAD54019.1.
AY424269 mRNA. Translation: AAR29061.1.
AY424270 mRNA. Translation: AAR29062.1.
AY339601 mRNA. Translation: AAQ02673.1.
AB037663 mRNA. Translation: BAB21504.1.
AK314443 mRNA. Translation: BAG37052.1.
AC020634 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79439.1.
BC100761 mRNA. Translation: AAI00762.2.
BC100762 mRNA. Translation: AAI00763.2.
X90870 mRNA. Translation: CAA62378.1.

IPI

IPI00221255.
IPI00221259.
IPI00336081.
IPI00736561.
IPI00791032.
IPI00791924.
IPI00855853.
IPI00955810.

RefSeq

NP_444253.3. NM_053025.3.
NP_444254.3. NM_053026.3.
NP_444255.3. NM_053027.3.
NP_444256.3. NM_053028.3.
NP_444259.1. NM_053031.2.
NP_444260.1. NM_053032.2.

UniGene

Hs.477375.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQV	NMR	-	A	1238-1338	[»]
2K0F	NMR	-	B	1742-1760	[»]
2YR3	NMR	-	A	510-601	[»]

ProteinModelPortal

Q15746.

SMR

Q15746. Positions 510-601, 1238-1338, 1801-1902.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15746. 9 interactions.

MINT

MINT-2807402.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

Q15746.

Polymorphism databases

DMDM

300669714.

Proteomic databases

PaxDb

Q15746.

PRIDE

Q15746.

Protocols and materials databases

DNASU

4638.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346322; ENSP00000320622; ENSG00000065534.
ENST00000359169; ENSP00000352088; ENSG00000065534.
ENST00000360304; ENSP00000353452; ENSG00000065534.
ENST00000360772; ENSP00000354004; ENSG00000065534.
ENST00000418370; ENSP00000428967; ENSG00000065534.
ENST00000475616; ENSP00000418335; ENSG00000065534.
ENST00000583087; ENSP00000462118; ENSG00000065534.

GeneID

4638.

KEGG

hsa:4638.

UCSC

uc003ego.3. human.
uc003egp.3. human.
uc003egq.3. human.
uc003egr.3. human.
uc011bjw.2. human.

Organism-specific databases

CTD

4638.

GeneCards

GC03M123281.

HGNC

HGNC:7590. MYLK.

HPA

CAB009628.
CAB020789.
HPA031677.

MIM

600922. gene.
613780. phenotype.

neXtProt

NX_Q15746.

Orphanet

91387. Familial thoracic aortic aneurysm.

PharmGKB

PA31388.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG052551.

InParanoid

Q15746.

KO

K00907.

OMA

KFIILSQ.

Enzyme and pathway databases

BRENDA

2.7.11.18. 2681.

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.

Reactome

REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpress

Q15746.

Bgee

Q15746.

Genevestigator

Q15746.

GermOnline

ENSG00000065534. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 10 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR020675. Myosin_light_ch_kinase-rel.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR22964. PTHR22964. 1 hit.

Pfam

PF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50853. 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]

ProtoNet

Search...

Other

BindingDB

Q15746.

ChEMBL

CHEMBL2428.

ChiTaRS

MYLK. human.

EvolutionaryTrace

Q15746.

GenomeRNAi

4638.

NextBio

17860.

SOURCE

Search...

Entry information

Entry name

MYLK_HUMAN

Accession

Primary (citable) accession number: Q15746
Secondary accession number(s): O95796 , O95797, O95798, O95799, Q14844, Q16794, Q3ZCP9, Q5MY99, Q5MYA0, Q7Z4J0, Q9C0L5, Q9UBG5, Q9UBY6, Q9UIT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 13, 2010
Last modified:	May 1, 2013
This is version 146 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.