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Q15746

- MYLK_HUMAN

UniProt

Q15746 - MYLK_HUMAN

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Protein

Myosin light chain kinase, smooth muscle

Gene

MYLK

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.13 Publications

Catalytic activityi

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

Cofactori

Magnesium.
Calcium.

Enzyme regulationi

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-9.6 Publications

Kineticsi

  1. KM=6.5 µM for MLC (isoform 1 at 22 degrees Celsius)1 Publication
  2. KM=7.2 µM for MLC (isoform 2 at 22 degrees Celsius)1 Publication

Vmax=11.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication

Vmax=10.9 µmol/min/mg enzyme (isoform 1 at 22 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1493 – 14931ATPPROSITE-ProRule annotation
Active sitei1585 – 15851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1470 – 14789ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: RefGenome
  3. metal ion binding Source: UniProtKB-KW
  4. myosin light chain kinase activity Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: RefGenome
  2. aorta smooth muscle tissue morphogenesis Source: BHF-UCL
  3. bleb assembly Source: UniProtKB
  4. cellular hypotonic response Source: UniProtKB
  5. muscle contraction Source: Reactome
  6. positive regulation of calcium ion transport Source: UniProtKB
  7. positive regulation of cell migration Source: UniProtKB
  8. positive regulation of wound healing Source: UniProtKB
  9. protein phosphorylation Source: ProtInc
  10. smooth muscle contraction Source: UniProtKB
  11. tonic smooth muscle contraction Source: UniProtKB
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. 2681.
ReactomeiREACT_20558. Smooth Muscle Contraction.
SignaLinkiQ15746.

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:MYLK
Synonyms:MLCK, MLCK1, MYLK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7590. MYLK.

Subcellular locationi

Cytoplasm. Cell projectionlamellipodium. Cleavage furrow. Cytoplasmcytoskeleton
Note: Localized to stress fibers during interphase and to the cleavage furrow during mitosis.

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cleavage furrow Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. lamellipodium Source: UniProtKB
  7. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Aortic aneurysm, familial 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1759 – 17591S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. 1 Publication
VAR_065577

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi608 – 6081K → A: Loss of acetylation and no kinase activity repression by NAA10/ARD1. 1 Publication

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

MIMi613780. phenotype.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBiPA31388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19141914Myosin light chain kinase, smooth musclePRO_0000024354Add
BLAST
Chaini1 – 19101910Myosin light chain kinase, smooth muscle, deglutamylated formBy similarityPRO_0000403731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi182 ↔ 233PROSITE-ProRule annotation
Modified residuei231 – 2311Phosphotyrosine; by ABL11 Publication
Modified residuei365 – 3651PhosphoserineBy similarity
Disulfide bondi435 ↔ 487PROSITE-ProRule annotation
Modified residuei464 – 4641Phosphotyrosine; by ABL1 and SRC3 Publications
Modified residuei471 – 4711Phosphotyrosine; by SRC2 Publications
Disulfide bondi535 ↔ 583PROSITE-ProRule annotation
Modified residuei556 – 5561Phosphotyrosine; by ABL11 Publication
Modified residuei608 – 6081N6-acetyllysine1 Publication
Modified residuei611 – 6111Phosphotyrosine; by ABL11 Publication
Disulfide bondi742 ↔ 805PROSITE-ProRule annotation
Modified residuei792 – 7921Phosphotyrosine; by ABL11 Publication
Modified residuei846 – 8461Phosphotyrosine; by ABL11 Publication
Disulfide bondi1119 ↔ 1170PROSITE-ProRule annotation
Modified residuei1438 – 14381Phosphoserine2 Publications
Modified residuei1449 – 14491Phosphotyrosine; by ABL11 Publication
Modified residuei1575 – 15751Phosphotyrosine; by ABL11 Publication
Modified residuei1635 – 16351Phosphotyrosine; by ABL11 Publication
Modified residuei1760 – 17601PhosphoserineBy similarity
Modified residuei1776 – 17761PhosphoserineBy similarity
Disulfide bondi1830 ↔ 1882PROSITE-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-464 and Tyr-471 promotes CTTN binding.5 Publications
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).By similarity
Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ15746.
PaxDbiQ15746.
PRIDEiQ15746.

PTM databases

PhosphoSiteiQ15746.

Expressioni

Tissue specificityi

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).4 Publications

Inductioni

Accumulates in individuals with asthma (at protein levels). Induced by tumor necrosis factor (TNF). Repressed by androgens (e.g. R1881).3 Publications

Gene expression databases

BgeeiQ15746.
ExpressionAtlasiQ15746. baseline and differential.
GenevestigatoriQ15746.

Organism-specific databases

HPAiCAB009628.
CAB020789.
HPA031677.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-968482,EBI-389883

Protein-protein interaction databases

BioGridi110722. 10 interactions.
IntActiQ15746. 11 interactions.
MINTiMINT-2807402.

Structurei

Secondary structure

1
1914
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi512 – 5187
Beta strandi523 – 5264
Beta strandi531 – 5344
Beta strandi536 – 5416
Beta strandi546 – 5538
Beta strandi560 – 5623
Beta strandi565 – 5706
Beta strandi581 – 5866
Beta strandi591 – 5955
Beta strandi598 – 6014
Beta strandi1239 – 12413
Beta strandi1246 – 12505
Beta strandi1255 – 126612
Beta strandi1268 – 127710
Beta strandi1281 – 12888
Beta strandi1290 – 12978
Turni1302 – 13043
Beta strandi1306 – 13138
Beta strandi1318 – 13203
Beta strandi1323 – 13286
Helixi1743 – 175917

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQVNMR-A1238-1338[»]
2K0FNMR-B1742-1760[»]
2YR3NMR-A510-601[»]
ProteinModelPortaliQ15746.
SMRiQ15746. Positions 510-601, 1238-1338, 1801-1902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15746.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12290Ig-like C2-type 1Add
BLAST
Domaini161 – 24989Ig-like C2-type 2Add
BLAST
Domaini414 – 50390Ig-like C2-type 3Add
BLAST
Domaini514 – 59986Ig-like C2-type 4Add
BLAST
Domaini620 – 71192Ig-like C2-type 5Add
BLAST
Domaini721 – 821101Ig-like C2-type 6Add
BLAST
Repeati868 – 895281-1Add
BLAST
Repeati896 – 923281-2Add
BLAST
Repeati924 – 951281-3Add
BLAST
Repeati952 – 979281-4Add
BLAST
Repeati980 – 998191-5; truncatedAdd
BLAST
Repeati999 – 100352-1; truncated
Repeati1004 – 1015122-2Add
BLAST
Repeati1016 – 1027122-3Add
BLAST
Repeati1028 – 1039122-4Add
BLAST
Repeati1040 – 1051122-5Add
BLAST
Repeati1052 – 1063122-6Add
BLAST
Domaini1098 – 118689Ig-like C2-type 7Add
BLAST
Domaini1238 – 132689Ig-like C2-type 8Add
BLAST
Domaini1334 – 142693Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini1464 – 1719256Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1809 – 189890Ig-like C2-type 9Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni868 – 9981315 X 28 AA approximate tandem repeatsAdd
BLAST
Regioni923 – 96341Actin-binding (calcium/calmodulin-sensitive)By similarityAdd
BLAST
Regioni948 – 96316Calmodulin-bindingBy similarityAdd
BLAST
Regioni999 – 1063656 X 12 AA approximate tandem repeatsAdd
BLAST
Regioni1061 – 1460400Actin-binding (calcium/calmodulin-insensitive)By similarityAdd
BLAST
Regioni1711 – 177464Calmodulin-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1906 – 19149Poly-Glu

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000049287.
HOVERGENiHBG052551.
InParanoidiQ15746.
KOiK00907.
OMAiKFIILSQ.
OrthoDBiEOG7WQ7RC.
PhylomeDBiQ15746.
TreeFamiTF314166.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view]
PANTHERiPTHR22964. PTHR22964. 1 hit.
PTHR22964:SF44. PTHR22964:SF44. 1 hit.
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. 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 (11)i

Sequence statusi: Complete.

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

This entry describes 11 isoformsi produced by alternative splicing and alternative initiation. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q15746-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGDVKLVASS HISKTSLSVD PSRVDSMPLT EAPAFILPPR NLCIKEGATA
60 70 80 90 100
KFEGRVRGYP EPQVTWHRNG QPITSGGRFL LDCGIRGTFS LVIHAVHEED
110 120 130 140 150
RGKYTCEATN GSGARQVTVE LTVEGSFAKQ LGQPVVSKTL GDRFSAPAVE
160 170 180 190 200
TRPSIWGECP PKFATKLGRV VVKEGQMGRF SCKITGRPQP QVTWLKGNVP
210 220 230 240 250
LQPSARVSVS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG KASMSAELSI
260 270 280 290 300
QGLDSANRSF VRETKATNSD VRKEVTNVIS KESKLDSLEA AAKSKNCSSP
310 320 330 340 350
QRGGSPPWAA NSQPQPPRES KLESCKDSPR TAPQTPVLQK TSSSITLQAA
360 370 380 390 400
RVQPEPRAPG LGVLSPSGEE RKRPAPPRPA TFPTRQPGLG SQDVVSKAAN
410 420 430 440 450
RRIPMEGQRD SAFPKFESKP QSQEVKENQT VKFRCEVSGI PKPEVAWFLE
460 470 480 490 500
GTPVRRQEGS IEVYEDAGSH YLCLLKARTR DSGTYSCTAS NAQGQLSCSW
510 520 530 540 550
TLQVERLAVM EVAPSFSSVL KDCAVIEGQD FVLQCSVRGT PVPRITWLLN
560 570 580 590 600
GQPIQYARST CEAGVAELHI QDALPEDHGT YTCLAENALG QVSCSAWVTV
610 620 630 640 650
HEKKSSRKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP
660 670 680 690 700
PPEVIWLHNG NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS
710 720 730 740 750
AGEVRTQAVL TVQEPHDGTQ PWFISKPRSV TASLGQSVLI SCAIAGDPFP
760 770 780 790 800
TVHWLRDGKA LCKDTGHFEV LQNEDVFTLV LKKVQPWHAG QYEILLKNRV
810 820 830 840 850
GECSCQVSLM LQNSSARALP RGREPASCED LCGGGVGADG GGSDRYGSLR
860 870 880 890 900
PGWPARGQGW LEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
910 920 930 940 950
LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ
960 970 980 990 1000
VDFRSVLAKK GTSKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA
1010 1020 1030 1040 1050
ETLNAKAVES SKPLSNAQPS GPLKPVGNAK PAETLKPMGN AKPAETLKPM
1060 1070 1080 1090 1100
GNAKPDENLK SASKEELKKD VKNDVNCKRG HAGTTDNEKR SESQGTAPAF
1110 1120 1130 1140 1150
KQKLQDVHVA EGKKLLLQCQ VSSDPPATII WTLNGKTLKT TKFIILSQEG
1160 1170 1180 1190 1200
SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CSCQVTVDDA PASENTKAPE
1210 1220 1230 1240 1250
MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR
1260 1270 1280 1290 1300
AGESVELFGK VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA
1310 1320 1330 1340 1350
RQEHCGCYTL LVENKLGSRQ AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL
1360 1370 1380 1390 1400
SWYGSSYDGG SAVQSYSIEI WDSANKTWKE LATCRSTSFN VQDLLPDHEY
1410 1420 1430 1440 1450
KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD DEKEPEVDYR
1460 1470 1480 1490 1500
TVTINTEQKV SDFYDIEERL GSGKFGQVFR LVEKKTRKVW AGKFFKAYSA
1510 1520 1530 1540 1550
KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI
1560 1570 1580 1590 1600
IDEDFELTER ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR
1610 1620 1630 1640 1650
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ATDMWSIGVI
1660 1670 1680 1690 1700
CYILVSGLSP FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL
1710 1720 1730 1740 1750
KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM ARRKWQKTGN
1760 1770 1780 1790 1800
AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV
1810 1820 1830 1840 1850
AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR
1860 1870 1880 1890 1900
ESRHFQIDYD EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE
1910
TMEEGEGEGE EEEE
Length:1,914
Mass (Da):210,715
Last modified:July 13, 2010 - v4
Checksum:i2D094E161CE2D4BA
GO
Isoform 2 (identifier: Q15746-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,845
Mass (Da):203,055
Checksum:i0111D4C5A88349AB
GO
Isoform 3A (identifier: Q15746-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,863
Mass (Da):205,059
Checksum:iA526210F1B9E546C
GO
Isoform 3B (identifier: Q15746-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,794
Mass (Da):197,399
Checksum:i9EE35F5BADBB0D9A
GO
Isoform 4 (identifier: Q15746-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,841
Mass (Da):202,350
Checksum:i23EDB48D1A11DE70
GO
Isoform Del-1790 (identifier: Q15746-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,913
Mass (Da):210,586
Checksum:i6D3029D5CCA13B41
GO
Isoform 5 (identifier: Q15746-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:992
Mass (Da):110,205
Checksum:i27288359F94FE260
GO
Isoform 6 (identifier: Q15746-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:154
Mass (Da):16,970
Checksum:i0E3B6CAD36C563EE
GO
Isoform 7 (identifier: Q15746-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1200: Missing.

Show »
Length:714
Mass (Da):80,410
Checksum:i5C3E8AD06D8B855D
GO
Isoform 8 (identifier: Q15746-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1760: Missing.
     1790-1790: Missing.

Note: Produced by alternative initiation at Met-1761 of isoform 1.

Show »
Length:153
Mass (Da):16,840
Checksum:iBF1292FFEB166F7B
GO
Isoform 9 (identifier: Q15746-11) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-922: Missing.
     1790-1790: Missing.

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

Show »
Length:991
Mass (Da):110,076
Checksum:iBCFD66306197E14C
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471P → S in AAC18423. (PubMed:9160829)Curated
Sequence conflicti147 – 1471P → S in AAD15922. (PubMed:10198165)Curated
Sequence conflicti147 – 1471P → S in AAD15923. (PubMed:10198165)Curated
Sequence conflicti147 – 1471P → S in AAR29062. (PubMed:15507455)Curated
Sequence conflicti147 – 1471P → S in AAQ02673. (PubMed:15020676)Curated
Sequence conflicti147 – 1471P → S in EAW79438. 1 PublicationCurated
Sequence conflicti147 – 1471P → S in EAW79440. 1 PublicationCurated
Sequence conflicti466 – 4661D → N in AAR29062. (PubMed:15507455)Curated
Sequence conflicti496 – 4961L → V in AAC18423. (PubMed:9160829)Curated
Sequence conflicti496 – 4961L → V in AAD15922. (PubMed:10198165)Curated
Sequence conflicti496 – 4961L → V in AAR29062. (PubMed:15507455)Curated
Sequence conflicti496 – 4961L → V in AAQ02673. (PubMed:15020676)Curated
Sequence conflicti681 – 6811C → W in AAC18423. (PubMed:9160829)Curated
Sequence conflicti681 – 6811C → W in AAD15921. (PubMed:10198165)Curated
Sequence conflicti681 – 6811C → W in AAD15922. (PubMed:10198165)Curated
Sequence conflicti681 – 6811C → W in AAD15923. (PubMed:10198165)Curated
Sequence conflicti933 – 9331V → M in CAA59685. (PubMed:8575746)Curated
Sequence conflicti963 – 9631S → P in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1022 – 10221P → A in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1048 – 10503KPM → EAH in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1048 – 10503KPM → EAH in BAB21504. 1 PublicationCurated
Sequence conflicti1162 – 11621P → L in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1162 – 11621P → L in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1210 – 12101L → P in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1280 – 12801E → D in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1280 – 12801E → D in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1284 – 12841M → I in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1284 – 12841M → I in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1284 – 12841M → I in AAD15924. (PubMed:10198165)Curated
Sequence conflicti1300 – 13001A → G in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1316 – 13161L → S in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1326 – 13261T → S in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1478 – 14781V → C in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1511 – 15111S → T in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1511 – 15111S → T in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1518 – 15181H → P in AAR29061. (PubMed:15507455)Curated
Sequence conflicti1518 – 15181H → P in AAR29062. (PubMed:15507455)Curated
Sequence conflicti1563 – 15631I → T in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1609 – 16091A → P in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1634 – 16341N → I in AAR29061. (PubMed:15507455)Curated
Sequence conflicti1634 – 16341N → I in AAR29062. (PubMed:15507455)Curated
Sequence conflicti1639 – 16402GY → D in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1639 – 16402GY → D in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1639 – 16402GY → D in AAD15924. (PubMed:10198165)Curated
Sequence conflicti1639 – 16391G → R in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1648 – 16481G → R in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1658 – 16592LS → PF in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1676 – 16761A → P in AAR29061. (PubMed:15507455)Curated
Sequence conflicti1676 – 16761A → P in AAR29062. (PubMed:15507455)Curated
Sequence conflicti1710 – 17112CT → LA in CAA59685. (PubMed:8575746)Curated
Sequence conflicti1897 – 18971L → H in AAD15922. (PubMed:10198165)Curated
Sequence conflicti1897 – 18971L → H in AAD15923. (PubMed:10198165)Curated
Sequence conflicti1897 – 18971L → H in AAD15924. (PubMed:10198165)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211P → H.
Corresponds to variant rs28497577 [ dbSNP | Ensembl ].
VAR_057106
Natural varianti128 – 1281A → V.1 Publication
Corresponds to variant rs143896146 [ dbSNP | Ensembl ].
VAR_065570
Natural varianti133 – 1331Q → H.1 Publication
Corresponds to variant rs140148380 [ dbSNP | Ensembl ].
VAR_065571
Natural varianti160 – 1601P → R.1 Publication
Corresponds to variant rs111256888 [ dbSNP | Ensembl ].
VAR_065572
Natural varianti261 – 2611V → A.1 Publication
Corresponds to variant rs3796164 [ dbSNP | Ensembl ].
VAR_040847
Natural varianti276 – 2761T → A.1 Publication
VAR_040848
Natural varianti336 – 3361P → L.
Corresponds to variant rs35912339 [ dbSNP | Ensembl ].
VAR_057107
Natural varianti378 – 3781R → H.1 Publication
VAR_040849
Natural varianti405 – 4051M → V.1 Publication
Corresponds to variant rs35436690 [ dbSNP | Ensembl ].
VAR_040850
Natural varianti443 – 4431P → S.1 Publication
Corresponds to variant rs35156360 [ dbSNP | Ensembl ].
VAR_040851
Natural varianti607 – 6071R → G.1 Publication
VAR_040852
Natural varianti652 – 6521P → A.1 Publication
VAR_040853
Natural varianti656 – 6561W → C.2 Publications
Corresponds to variant rs138172035 [ dbSNP | Ensembl ].
VAR_040854
Natural varianti692 – 6921T → M.1 Publication
VAR_040855
Natural varianti701 – 7011A → T.1 Publication
Corresponds to variant rs142835596 [ dbSNP | Ensembl ].
VAR_040856
Natural varianti709 – 7091V → M.1 Publication
VAR_040857
Natural varianti845 – 8451R → C.
Corresponds to variant rs3732485 [ dbSNP | Ensembl ].
VAR_057108
Natural varianti861 – 8611L → P.
Corresponds to variant rs3732486 [ dbSNP | Ensembl ].
VAR_019986
Natural varianti877 – 8771V → M.
Corresponds to variant rs34542174 [ dbSNP | Ensembl ].
VAR_057109
Natural varianti914 – 9141D → E.
Corresponds to variant rs3732487 [ dbSNP | Ensembl ].
VAR_019987
Natural varianti1085 – 10851T → A.1 Publication
Corresponds to variant rs75370906 [ dbSNP | Ensembl ].
VAR_065573
Natural varianti1213 – 12131V → M Found in a patient with familial aortic dissections. 1 Publication
VAR_065574
Natural varianti1399 – 13991E → K Found in a patient with familial aortic dissections. 1 Publication
Corresponds to variant rs181663420 [ dbSNP | Ensembl ].
VAR_065575
Natural varianti1527 – 15271A → V.1 Publication
VAR_040858
Natural varianti1588 – 15881P → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040859
Natural varianti1754 – 17541A → T Found in a patient with familial aortic dissections; binding to calmodulin is reduced; significant reduction in kinase activity compared to wild-type protein. 1 Publication
VAR_065576
Natural varianti1759 – 17591S → P in AAT7; shows minimal cells endogenous expression; binding to calmodulin is abolished; 6-fold reduction in kinase activity compared to wild-type protein. 1 Publication
VAR_065577

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17601760Missing in isoform 6 and isoform 8. 3 PublicationsVSP_018846Add
BLAST
Alternative sequencei1 – 12001200Missing in isoform 7. 1 PublicationVSP_053791Add
BLAST
Alternative sequencei1 – 922922Missing in isoform 5 and isoform 9. 2 PublicationsVSP_018845Add
BLAST
Alternative sequencei437 – 50670VSGIP…LQVER → G in isoform 2 and isoform 3B. 2 PublicationsVSP_004791Add
BLAST
Alternative sequencei1473 – 154573Missing in isoform 4. 1 PublicationVSP_004793Add
BLAST
Alternative sequencei1655 – 170551Missing in isoform 3A and isoform 3B. 1 PublicationVSP_004794Add
BLAST
Alternative sequencei1790 – 17901Missing in isoform Del-1790, isoform 8 and isoform 9. 4 PublicationsVSP_004795

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
AK300610 mRNA. Translation: BAG62305.1.
AK314412 mRNA. Translation: BAG37033.1.
AK314443 mRNA. Translation: BAG37052.1.
AC020634 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79438.1.
CH471052 Genomic DNA. Translation: EAW79439.1.
CH471052 Genomic DNA. Translation: EAW79440.1.
CH471052 Genomic DNA. Translation: EAW79441.1.
BC100761 mRNA. Translation: AAI00762.2.
BC100762 mRNA. Translation: AAI00763.2.
BC100763 mRNA. Translation: AAI00764.2.
BC064420 mRNA. Translation: AAH64420.2.
X90870 mRNA. Translation: CAA62378.1.
CCDSiCCDS3023.1. [Q15746-3]
CCDS43141.1. [Q15746-2]
CCDS46896.1. [Q15746-1]
CCDS46897.1. [Q15746-8]
CCDS58849.1. [Q15746-10]
RefSeqiNP_444253.3. NM_053025.3. [Q15746-1]
NP_444254.3. NM_053026.3. [Q15746-2]
NP_444255.3. NM_053027.3. [Q15746-3]
NP_444256.3. NM_053028.3. [Q15746-4]
NP_444259.1. NM_053031.2. [Q15746-10]
NP_444260.1. NM_053032.2. [Q15746-8]
UniGeneiHs.477375.

Genome annotation databases

EnsembliENST00000346322; ENSP00000320622; ENSG00000065534. [Q15746-2]
ENST00000354792; ENSP00000346846; ENSG00000065534. [Q15746-2]
ENST00000359169; ENSP00000352088; ENSG00000065534. [Q15746-3]
ENST00000360304; ENSP00000353452; ENSG00000065534. [Q15746-1]
ENST00000360772; ENSP00000354004; ENSG00000065534. [Q15746-3]
ENST00000418370; ENSP00000428967; ENSG00000065534. [Q15746-8]
ENST00000475616; ENSP00000418335; ENSG00000065534. [Q15746-1]
ENST00000578202; ENSP00000463691; ENSG00000065534. [Q15746-10]
ENST00000583087; ENSP00000462118; ENSG00000065534. [Q15746-8]
GeneIDi4638.
KEGGihsa:4638.
UCSCiuc003egl.3. human. [Q15746-8]
uc003egm.3. human.
uc003ego.3. human. [Q15746-1]
uc003egp.3. human. [Q15746-2]
uc003egq.3. human. [Q15746-3]
uc003egr.3. human. [Q15746-4]
uc011bjv.2. human.
uc011bjw.2. human. [Q15746-6]

Polymorphism databases

DMDMi300669714.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Myosin light-chain kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
AK300610 mRNA. Translation: BAG62305.1 .
AK314412 mRNA. Translation: BAG37033.1 .
AK314443 mRNA. Translation: BAG37052.1 .
AC020634 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79438.1 .
CH471052 Genomic DNA. Translation: EAW79439.1 .
CH471052 Genomic DNA. Translation: EAW79440.1 .
CH471052 Genomic DNA. Translation: EAW79441.1 .
BC100761 mRNA. Translation: AAI00762.2 .
BC100762 mRNA. Translation: AAI00763.2 .
BC100763 mRNA. Translation: AAI00764.2 .
BC064420 mRNA. Translation: AAH64420.2 .
X90870 mRNA. Translation: CAA62378.1 .
CCDSi CCDS3023.1. [Q15746-3 ]
CCDS43141.1. [Q15746-2 ]
CCDS46896.1. [Q15746-1 ]
CCDS46897.1. [Q15746-8 ]
CCDS58849.1. [Q15746-10 ]
RefSeqi NP_444253.3. NM_053025.3. [Q15746-1 ]
NP_444254.3. NM_053026.3. [Q15746-2 ]
NP_444255.3. NM_053027.3. [Q15746-3 ]
NP_444256.3. NM_053028.3. [Q15746-4 ]
NP_444259.1. NM_053031.2. [Q15746-10 ]
NP_444260.1. NM_053032.2. [Q15746-8 ]
UniGenei Hs.477375.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQV NMR - A 1238-1338 [» ]
2K0F NMR - B 1742-1760 [» ]
2YR3 NMR - A 510-601 [» ]
ProteinModelPortali Q15746.
SMRi Q15746. Positions 510-601, 1238-1338, 1801-1902.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110722. 10 interactions.
IntActi Q15746. 11 interactions.
MINTi MINT-2807402.

Chemistry

BindingDBi Q15746.
ChEMBLi CHEMBL2428.
GuidetoPHARMACOLOGYi 1552.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q15746.

Polymorphism databases

DMDMi 300669714.

Proteomic databases

MaxQBi Q15746.
PaxDbi Q15746.
PRIDEi Q15746.

Protocols and materials databases

DNASUi 4638.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346322 ; ENSP00000320622 ; ENSG00000065534 . [Q15746-2 ]
ENST00000354792 ; ENSP00000346846 ; ENSG00000065534 . [Q15746-2 ]
ENST00000359169 ; ENSP00000352088 ; ENSG00000065534 . [Q15746-3 ]
ENST00000360304 ; ENSP00000353452 ; ENSG00000065534 . [Q15746-1 ]
ENST00000360772 ; ENSP00000354004 ; ENSG00000065534 . [Q15746-3 ]
ENST00000418370 ; ENSP00000428967 ; ENSG00000065534 . [Q15746-8 ]
ENST00000475616 ; ENSP00000418335 ; ENSG00000065534 . [Q15746-1 ]
ENST00000578202 ; ENSP00000463691 ; ENSG00000065534 . [Q15746-10 ]
ENST00000583087 ; ENSP00000462118 ; ENSG00000065534 . [Q15746-8 ]
GeneIDi 4638.
KEGGi hsa:4638.
UCSCi uc003egl.3. human. [Q15746-8 ]
uc003egm.3. human.
uc003ego.3. human. [Q15746-1 ]
uc003egp.3. human. [Q15746-2 ]
uc003egq.3. human. [Q15746-3 ]
uc003egr.3. human. [Q15746-4 ]
uc011bjv.2. human.
uc011bjw.2. human. [Q15746-6 ]

Organism-specific databases

CTDi 4638.
GeneCardsi GC03M123281.
GeneReviewsi MYLK.
HGNCi HGNC:7590. MYLK.
HPAi CAB009628.
CAB020789.
HPA031677.
MIMi 600922. gene.
613780. phenotype.
neXtProti NX_Q15746.
Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBi PA31388.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118877.
HOGENOMi HOG000049287.
HOVERGENi HBG052551.
InParanoidi Q15746.
KOi K00907.
OMAi KFIILSQ.
OrthoDBi EOG7WQ7RC.
PhylomeDBi Q15746.
TreeFami TF314166.

Enzyme and pathway databases

BRENDAi 2.7.11.18. 2681.
Reactomei REACT_20558. Smooth Muscle Contraction.
SignaLinki Q15746.

Miscellaneous databases

ChiTaRSi MYLK. human.
EvolutionaryTracei Q15746.
GeneWikii MYLK.
GenomeRNAii 4638.
NextBioi 17860.
PROi Q15746.
SOURCEi Search...

Gene expression databases

Bgeei Q15746.
ExpressionAtlasi Q15746. baseline and differential.
Genevestigatori Q15746.

Family and domain databases

Gene3Di 2.60.40.10. 10 hits.
InterProi 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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
IPR015725. Telokin/Myosin_light_ch_kin.
[Graphical view ]
PANTHERi PTHR22964. PTHR22964. 1 hit.
PTHR22964:SF44. PTHR22964:SF44. 1 hit.
Pfami PF00041. fn3. 1 hit.
PF07679. I-set. 9 hits.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 9), 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 AND 3B), NUCLEOTIDE SEQUENCE [MRNA] OF 1281-1914 (ISOFORM 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] (ISOFORM 8), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1614-1914 (ISOFORM 9/DEL-1790), 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] (ISOFORMS 6; 7 AND 8).
    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. 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] (ISOFORMS 6 AND 8).
  13. Watterson D.M.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1456-1914 (ISOFORM 9/DEL-1790).
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. Cited for: FUNCTION IN INFLAMMATORY RESPONSE.
  34. "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.
  35. "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.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "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.
  38. "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.
  39. "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.
  40. 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.

Entry informationi

Entry nameiMYLK_HUMAN
AccessioniPrimary (citable) accession number: Q15746
Secondary accession number(s): B4DUE3
, D3DN97, O95796, O95797, O95798, O95799, Q14844, Q16794, Q17S15, Q3ZCP9, Q5MY99, Q5MYA0, Q6P2N0, Q7Z4J0, Q9C0L5, Q9UBG5, Q9UBY6, Q9UIT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3