Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q14680

- MELK_HUMAN

UniProt

Q14680 - MELK_HUMAN

Protein

Maternal embryonic leucine zipper kinase

Gene

MELK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (19 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.6 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation
    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Activated by autophosphorylation of the T-loop at Thr-167 and Ser-171: in contrast to other members of the SNF1 subfamily, phosphorylation at Thr-167 is not mediated by STK11/LKB1 but via autophosphorylation instead. Inhibited by calcium-binding. Kinase activity is also regulated by reducing agents: dithiothreitol (DTT) or reduced glutathione are required for kinase activity in vitro; such dependence is however not due to the presence of disulfide bonds.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401ATPPROSITE-ProRule annotation
    Active sitei132 – 1321Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 259ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: UniProtKB
    3. lipid binding Source: UniProtKB-KW
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell proliferation Source: UniProtKB
    3. G2/M transition of mitotic cell cycle Source: UniProtKB
    4. hemopoiesis Source: UniProtKB
    5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
    6. neural precursor cell proliferation Source: UniProtKB
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. positive regulation of apoptotic process Source: UniProtKB
    9. protein autophosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Calcium, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ14680.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maternal embryonic leucine zipper kinase (EC:2.7.11.1)
    Short name:
    hMELK
    Alternative name(s):
    Protein kinase Eg3
    Short name:
    pEg3 kinase
    Protein kinase PK38
    Short name:
    hPK38
    Tyrosine-protein kinase MELK (EC:2.7.10.2)
    Gene namesi
    Name:MELK
    Synonyms:KIAA0175
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:16870. MELK.

    Subcellular locationi

    Cell membrane 2 Publications; Peripheral membrane protein 2 Publications

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. membrane Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in MELK are associated with some cancers, such as brain or breast cancers. Expression is dramatically increased in aggressive undifferentiated tumors, correlating with poor patient outcome in breast and brain cancers, suggesting a role in tumor-initiating cells and proliferation via its function in cell proliferation regulation.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291C → V: Abolishes dependence to reducing agents; when associated with V-70; A-89; A-154; A-168; A-169; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi70 – 701C → V: Abolishes dependence to reducing agents; when associated with V-29; A-89; A-154; A-168; A-169; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi89 – 891C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-154; A-168; A-169; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi150 – 1501D → A: Abolishes enzymatic activity. 3 Publications
    Mutagenesisi154 – 1541C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-168; A-169; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi163 – 1631Y → F: Abolishes autophosphorylation on tyrosine but still active on exogenous substrates. 1 Publication
    Mutagenesisi167 – 1671T → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. 1 Publication
    Mutagenesisi167 – 1671T → D or E: Phosphomimetic mutant that has similar kinase activity as wild-type. 1 Publication
    Mutagenesisi168 – 1681C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-169; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi169 – 1691C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-204; A-286 and A-339. 1 Publication
    Mutagenesisi171 – 1711S → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. 1 Publication
    Mutagenesisi171 – 1711S → D: Inactive. 1 Publication
    Mutagenesisi204 – 2041C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-286 and A-339. 1 Publication
    Mutagenesisi283 – 2853DDD → KKK: Inactive.
    Mutagenesisi286 – 2861C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339. 1 Publication
    Mutagenesisi339 – 3391C → A: Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204 and A-286. 1 Publication
    Mutagenesisi345 – 3451T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi387 – 3871T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi409 – 4091T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi415 – 4151T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi428 – 4281T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi446 – 4461T → A: Inhibits interaction with PPP1R8. 1 Publication
    Mutagenesisi460 – 4601T → A: Inhibits interaction with PPP1R8. 1 Publication
    Mutagenesisi466 – 4661T → A: Inhibits interaction with PPP1R8. 1 Publication
    Mutagenesisi478 – 4781T → A: Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity. 1 Publication
    Mutagenesisi518 – 5181T → A: No effect on interaction with PPP1R8. 1 Publication

    Organism-specific databases

    PharmGKBiPA134902874.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Maternal embryonic leucine zipper kinasePRO_0000086323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561Phosphothreonine; by autocatalysis2 Publications
    Modified residuei163 – 1631Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei167 – 1671Phosphothreonine; by autocatalysis4 Publications
    Modified residuei171 – 1711Phosphoserine; by autocatalysis2 Publications
    Modified residuei253 – 2531Phosphoserine; by autocatalysis2 Publications
    Modified residuei336 – 3361Phosphoserine; by autocatalysis2 Publications
    Modified residuei343 – 3431Phosphoserine; by autocatalysis3 Publications
    Modified residuei356 – 3561Phosphoserine; by autocatalysis6 Publications
    Modified residuei367 – 3671Phosphotyrosine2 Publications
    Modified residuei391 – 3911Phosphoserine; by autocatalysis2 Publications
    Modified residuei398 – 3981Phosphothreonine; by autocatalysis3 Publications
    Modified residuei407 – 4071Phosphoserine; by autocatalysis2 Publications
    Modified residuei409 – 4091Phosphothreonine2 Publications
    Modified residuei431 – 4311Phosphoserine; by autocatalysis4 Publications
    Modified residuei478 – 4781Phosphothreonine2 Publications
    Modified residuei494 – 4941Phosphothreonine; by autocatalysis3 Publications
    Modified residuei498 – 4981Phosphoserine3 Publications
    Modified residuei505 – 5051Phosphoserine; by autocatalysis7 Publications
    Modified residuei518 – 5181Phosphothreonine2 Publications
    Modified residuei529 – 5291Phosphoserine; alternate5 Publications
    Modified residuei529 – 5291Phosphoserine; by autocatalysis; alternate5 Publications
    Modified residuei539 – 5391Phosphothreonine; by autocatalysis2 Publications

    Post-translational modificationi

    Autophosphorylated: autophosphorylation of the T-loop at Thr-167 and Ser-171 is required for activation. Thr-478 phosphorylation during mitosis promotes interaction with PPP1R8 Probable.10 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14680.
    PaxDbiQ14680.
    PRIDEiQ14680.

    PTM databases

    PhosphoSiteiQ14680.

    Expressioni

    Tissue specificityi

    Expressed in placenta, kidney, thymus, testis, ovary and intestine.1 Publication

    Developmental stagei

    Increases during G2/M phase compared to interphase. Protein level decreases when cells exit mitosis, probably due to degradation.1 Publication

    Inductioni

    Up-regulated in many cancers cells. Up-regulated upon treatment with radiation or 5-fluorouracil (5-FU) in colorectal cancer cells, suggesting that it might be associated with increased resistance of colorectal cells against radiation and 5-FU. Down-regulated upon siomycin A, a thiazole antibiotic, treatment, leading to inhibit tumor growth in vivo.2 Publications

    Gene expression databases

    ArrayExpressiQ14680.
    BgeeiQ14680.
    CleanExiHS_MELK.
    GenevestigatoriQ14680.

    Organism-specific databases

    HPAiHPA017214.

    Interactioni

    Subunit structurei

    Monomer. Interacts with ZNF622 and PPP1R8.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2L14Q9BZR84EBI-1046702,EBI-1385773

    Protein-protein interaction databases

    BioGridi115171. 10 interactions.
    IntActiQ14680. 3 interactions.
    MINTiMINT-7944803.
    STRINGi9606.ENSP00000298048.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Helixi7 – 93
    Beta strandi11 – 199
    Beta strandi21 – 3010
    Turni31 – 333
    Beta strandi36 – 4510
    Helixi48 – 503
    Helixi51 – 6212
    Beta strandi72 – 776
    Beta strandi79 – 879
    Helixi94 – 1018
    Helixi106 – 12520
    Helixi135 – 1373
    Beta strandi138 – 1403
    Beta strandi146 – 1483
    Beta strandi153 – 1586
    Turni159 – 1624
    Beta strandi163 – 1664
    Helixi172 – 1743
    Helixi177 – 1804
    Helixi188 – 20417
    Helixi214 – 22310
    Helixi234 – 24310
    Turni248 – 2503
    Helixi254 – 2585
    Helixi261 – 2644
    Turni265 – 2673
    Beta strandi279 – 2813
    Helixi284 – 29310
    Helixi298 – 3058
    Helixi312 – 32514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BKYX-ray1.83A2-340[»]
    4BKZX-ray2.20A2-340[»]
    4BL1X-ray2.60A2-340[»]
    4IXPX-ray2.75A1-340[»]
    ProteinModelPortaliQ14680.
    SMRiQ14680. Positions 2-335, 554-651.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 263253Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini602 – 65150KA1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni282 – 32140UBA-likeAdd
    BLAST
    Regioni326 – 651326Autoinhibitory regionAdd
    BLAST

    Domaini

    The KA1 domain mediates binding to phospholipids and targeting to membranes.By similarity

    Sequence similaritiesi

    Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233023.
    HOVERGENiHBG106273.
    InParanoidiQ14680.
    KOiK08799.
    OMAiWQSKNPF.
    OrthoDBiEOG7CK36C.
    PhylomeDBiQ14680.
    TreeFamiTF314032.

    Family and domain databases

    Gene3Di3.30.310.80. 1 hit.
    InterProiIPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14680-1) [UniParc]FASTAAdd to Basket

    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

    MKDYDELLKY YELHETIGTG GFAKVKLACH ILTGEMVAIK IMDKNTLGSD    50
    LPRIKTEIEA LKNLRHQHIC QLYHVLETAN KIFMVLEYCP GGELFDYIIS 100
    QDRLSEEETR VVFRQIVSAV AYVHSQGYAH RDLKPENLLF DEYHKLKLID 150
    FGLCAKPKGN KDYHLQTCCG SLAYAAPELI QGKSYLGSEA DVWSMGILLY 200
    VLMCGFLPFD DDNVMALYKK IMRGKYDVPK WLSPSSILLL QQMLQVDPKK 250
    RISMKNLLNH PWIMQDYNYP VEWQSKNPFI HLDDDCVTEL SVHHRNNRQT 300
    MEDLISLWQY DHLTATYLLL LAKKARGKPV RLRLSSFSCG QASATPFTDI 350
    KSNNWSLEDV TASDKNYVAG LIDYDWCEDD LSTGAATPRT SQFTKYWTES 400
    NGVESKSLTP ALCRTPANKL KNKENVYTPK SAVKNEEYFM FPEPKTPVNK 450
    NQHKREILTT PNRYTTPSKA RNQCLKETPI KIPVNSTGTD KLMTGVISPE 500
    RRCRSVELDL NQAHMEETPK RKGAKVFGSL ERGLDKVITV LTRSKRKGSA 550
    RDGPRRLKLH YNVTTTRLVN PDQLLNEIMS ILPKKHVDFV QKGYTLKCQT 600
    QSDFGKVTMQ FELEVCQLQK PDVVGIRRQR LKGDAWVYKR LVEDILSSCK 650
    V 651
    Length:651
    Mass (Da):74,642
    Last modified:July 19, 2004 - v3
    Checksum:i57F05CDC6122E570
    GO
    Isoform 2 (identifier: Q14680-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-158: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:580
    Mass (Da):66,399
    Checksum:iB91D7CA0BA90C2C1
    GO
    Isoform 3 (identifier: Q14680-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-194: Missing.

    Show »
    Length:457
    Mass (Da):52,528
    Checksum:i8E6CB0758D50AC49
    GO
    Isoform 4 (identifier: Q14680-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-135: MKDYDELLKY...QGYAHRDLKP → MVLE

    Show »
    Length:520
    Mass (Da):59,576
    Checksum:iF56647A88C371BBF
    GO
    Isoform 5 (identifier: Q14680-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-87: MKDYDELLKY...TANKIFMVLE → MMNFSNIMNYMKLLGQ

    Show »
    Length:580
    Mass (Da):66,547
    Checksum:i1A6547694E09401B
    GO
    Isoform 6 (identifier: Q14680-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLG → MMNFSNIMNYMKLLGQ

    Show »
    Length:619
    Mass (Da):71,174
    Checksum:iAF6938BF6FFB3CE4
    GO
    Isoform 7 (identifier: Q14680-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         352-392: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:610
    Mass (Da):70,150
    Checksum:i2A9A1C90DF1F63B9
    GO
    Isoform 8 (identifier: Q14680-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-135: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:603
    Mass (Da):69,116
    Checksum:iE1FEF6AD1C03F796
    GO

    Sequence cautioni

    The sequence BAA11492.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691I → M in BAH12961. (PubMed:14702039)Curated
    Sequence conflicti398 – 3981T → A in BAH12961. (PubMed:14702039)Curated
    Sequence conflicti428 – 4281T → A in BAH11482. (PubMed:14702039)Curated
    Sequence conflicti474 – 4741C → R in BAH13343. (PubMed:14702039)Curated
    Sequence conflicti483 – 4831P → L in BAH13354. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561T → M.1 Publication
    Corresponds to variant rs35233455 [ dbSNP | Ensembl ].
    VAR_040794
    Natural varianti219 – 2191K → R.1 Publication
    Corresponds to variant rs35142210 [ dbSNP | Ensembl ].
    VAR_040795
    Natural varianti333 – 3331R → K.1 Publication
    Corresponds to variant rs34655121 [ dbSNP | Ensembl ].
    VAR_040796
    Natural varianti348 – 3481T → I.1 Publication
    Corresponds to variant rs55845414 [ dbSNP | Ensembl ].
    VAR_040797
    Natural varianti460 – 4601T → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040798

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 194194Missing in isoform 3. 1 PublicationVSP_045208Add
    BLAST
    Alternative sequencei1 – 135135MKDYD…RDLKP → MVLE in isoform 4. 1 PublicationVSP_045209Add
    BLAST
    Alternative sequencei1 – 8787MKDYD…FMVLE → MMNFSNIMNYMKLLGQ in isoform 5. 2 PublicationsVSP_045430Add
    BLAST
    Alternative sequencei1 – 4848MKDYD…KNTLG → MMNFSNIMNYMKLLGQ in isoform 6. 1 PublicationVSP_045431Add
    BLAST
    Alternative sequencei88 – 15871Missing in isoform 2. 1 PublicationVSP_044715Add
    BLAST
    Alternative sequencei88 – 13548Missing in isoform 8. 1 PublicationVSP_046759Add
    BLAST
    Alternative sequencei352 – 39241Missing in isoform 7. 1 PublicationVSP_046760Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB183427 mRNA. Translation: BAF73615.1.
    AB183428 mRNA. Translation: BAF73616.1.
    D79997 mRNA. Translation: BAA11492.2. Different initiation.
    AK293284 mRNA. Translation: BAH11482.1.
    AK293447 mRNA. Translation: BAH11508.1.
    AK299164 mRNA. Translation: BAH12961.1.
    AK300761 mRNA. Translation: BAH13343.1.
    AK300821 mRNA. Translation: BAH13354.1.
    AK301131 mRNA. Translation: BAH13416.1.
    AK302374 mRNA. Translation: BAH13687.1.
    AL354932, AL442063 Genomic DNA. Translation: CAI11034.2.
    AL442063, AL354932 Genomic DNA. Translation: CAI16995.2.
    CH471071 Genomic DNA. Translation: EAW58303.1.
    CH471071 Genomic DNA. Translation: EAW58304.1.
    BC014039 mRNA. Translation: AAH14039.1.
    CCDSiCCDS59123.1. [Q14680-7]
    CCDS59124.1. [Q14680-8]
    CCDS59125.1. [Q14680-2]
    CCDS59126.1. [Q14680-6]
    CCDS59127.1. [Q14680-5]
    CCDS59128.1. [Q14680-4]
    CCDS59129.1. [Q14680-3]
    CCDS6606.1. [Q14680-1]
    RefSeqiNP_001243614.1. NM_001256685.1. [Q14680-7]
    NP_001243616.1. NM_001256687.1. [Q14680-8]
    NP_001243617.1. NM_001256688.1. [Q14680-2]
    NP_001243618.1. NM_001256689.1. [Q14680-6]
    NP_001243619.1. NM_001256690.1. [Q14680-5]
    NP_001243621.1. NM_001256692.1. [Q14680-4]
    NP_001243622.1. NM_001256693.1. [Q14680-3]
    NP_055606.1. NM_014791.3. [Q14680-1]
    UniGeneiHs.184339.

    Genome annotation databases

    EnsembliENST00000298048; ENSP00000298048; ENSG00000165304. [Q14680-1]
    ENST00000536329; ENSP00000443550; ENSG00000165304. [Q14680-5]
    ENST00000536860; ENSP00000439792; ENSG00000165304. [Q14680-8]
    ENST00000536987; ENSP00000439184; ENSG00000165304. [Q14680-4]
    ENST00000541717; ENSP00000437804; ENSG00000165304. [Q14680-7]
    ENST00000543751; ENSP00000441596; ENSG00000165304. [Q14680-6]
    ENST00000545008; ENSP00000445452; ENSG00000165304. [Q14680-2]
    GeneIDi9833.
    KEGGihsa:9833.
    UCSCiuc003zzn.4. human. [Q14680-1]
    uc011lpm.3. human.

    Polymorphism databases

    DMDMi50400857.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB183427 mRNA. Translation: BAF73615.1 .
    AB183428 mRNA. Translation: BAF73616.1 .
    D79997 mRNA. Translation: BAA11492.2 . Different initiation.
    AK293284 mRNA. Translation: BAH11482.1 .
    AK293447 mRNA. Translation: BAH11508.1 .
    AK299164 mRNA. Translation: BAH12961.1 .
    AK300761 mRNA. Translation: BAH13343.1 .
    AK300821 mRNA. Translation: BAH13354.1 .
    AK301131 mRNA. Translation: BAH13416.1 .
    AK302374 mRNA. Translation: BAH13687.1 .
    AL354932 , AL442063 Genomic DNA. Translation: CAI11034.2 .
    AL442063 , AL354932 Genomic DNA. Translation: CAI16995.2 .
    CH471071 Genomic DNA. Translation: EAW58303.1 .
    CH471071 Genomic DNA. Translation: EAW58304.1 .
    BC014039 mRNA. Translation: AAH14039.1 .
    CCDSi CCDS59123.1. [Q14680-7 ]
    CCDS59124.1. [Q14680-8 ]
    CCDS59125.1. [Q14680-2 ]
    CCDS59126.1. [Q14680-6 ]
    CCDS59127.1. [Q14680-5 ]
    CCDS59128.1. [Q14680-4 ]
    CCDS59129.1. [Q14680-3 ]
    CCDS6606.1. [Q14680-1 ]
    RefSeqi NP_001243614.1. NM_001256685.1. [Q14680-7 ]
    NP_001243616.1. NM_001256687.1. [Q14680-8 ]
    NP_001243617.1. NM_001256688.1. [Q14680-2 ]
    NP_001243618.1. NM_001256689.1. [Q14680-6 ]
    NP_001243619.1. NM_001256690.1. [Q14680-5 ]
    NP_001243621.1. NM_001256692.1. [Q14680-4 ]
    NP_001243622.1. NM_001256693.1. [Q14680-3 ]
    NP_055606.1. NM_014791.3. [Q14680-1 ]
    UniGenei Hs.184339.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BKY X-ray 1.83 A 2-340 [» ]
    4BKZ X-ray 2.20 A 2-340 [» ]
    4BL1 X-ray 2.60 A 2-340 [» ]
    4IXP X-ray 2.75 A 1-340 [» ]
    ProteinModelPortali Q14680.
    SMRi Q14680. Positions 2-335, 554-651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115171. 10 interactions.
    IntActi Q14680. 3 interactions.
    MINTi MINT-7944803.
    STRINGi 9606.ENSP00000298048.

    Chemistry

    BindingDBi Q14680.
    ChEMBLi CHEMBL4578.
    GuidetoPHARMACOLOGYi 2102.

    PTM databases

    PhosphoSitei Q14680.

    Polymorphism databases

    DMDMi 50400857.

    Proteomic databases

    MaxQBi Q14680.
    PaxDbi Q14680.
    PRIDEi Q14680.

    Protocols and materials databases

    DNASUi 9833.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298048 ; ENSP00000298048 ; ENSG00000165304 . [Q14680-1 ]
    ENST00000536329 ; ENSP00000443550 ; ENSG00000165304 . [Q14680-5 ]
    ENST00000536860 ; ENSP00000439792 ; ENSG00000165304 . [Q14680-8 ]
    ENST00000536987 ; ENSP00000439184 ; ENSG00000165304 . [Q14680-4 ]
    ENST00000541717 ; ENSP00000437804 ; ENSG00000165304 . [Q14680-7 ]
    ENST00000543751 ; ENSP00000441596 ; ENSG00000165304 . [Q14680-6 ]
    ENST00000545008 ; ENSP00000445452 ; ENSG00000165304 . [Q14680-2 ]
    GeneIDi 9833.
    KEGGi hsa:9833.
    UCSCi uc003zzn.4. human. [Q14680-1 ]
    uc011lpm.3. human.

    Organism-specific databases

    CTDi 9833.
    GeneCardsi GC09P036562.
    HGNCi HGNC:16870. MELK.
    HPAi HPA017214.
    MIMi 607025. gene.
    neXtProti NX_Q14680.
    PharmGKBi PA134902874.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233023.
    HOVERGENi HBG106273.
    InParanoidi Q14680.
    KOi K08799.
    OMAi WQSKNPF.
    OrthoDBi EOG7CK36C.
    PhylomeDBi Q14680.
    TreeFami TF314032.

    Enzyme and pathway databases

    SignaLinki Q14680.

    Miscellaneous databases

    GeneWikii MELK.
    GenomeRNAii 9833.
    NextBioi 35480044.
    PROi Q14680.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14680.
    Bgeei Q14680.
    CleanExi HS_MELK.
    Genevestigatori Q14680.

    Family and domain databases

    Gene3Di 3.30.310.80. 1 hit.
    InterProi IPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of MELK whose expression was highly up-regulated in breast cancers."
      Katagiri T., Lin M.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
    2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    3. "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 2; 3; 4; 5; 7 AND 8).
      Tissue: Spleen and Testis.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon.
    7. "Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine protein serine/threonine kinase 38 (MPK38)."
      Seong H.-A., Gil M., Kim K.-T., Kim S.-J., Ha H.
      Biochem. J. 361:597-604(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF622, FUNCTION IN PHOSPHORYLATION OF ZNF622.
      Tissue: Keratinocyte.
    8. "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation."
      Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.
      Oncogene 21:7630-7641(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25B.
    9. "Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1."
      Vulsteke V., Beullens M., Boudrez A., Keppens S., Van Eynde A., Rider M.H., Stalmans W., Bollen M.
      J. Biol. Chem. 279:8642-8647(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R8, AUTOPHOSPHORYLATION, MUTAGENESIS OF ASP-150; THR-345; THR-387; THR-409; THR-415; THR-428; THR-446; THR-460; THR-466; THR-478 AND THR-518, PHOSPHORYLATION AT THR-478, FUNCTION.
    10. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
      Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
      EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-167, AUTOPHOSPHORYLATION, MUTAGENESIS OF THR-167.
    11. "Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers."
      Gray D., Jubb A.M., Hogue D., Dowd P., Kljavin N., Yi S., Bai W., Frantz G., Zhang Z., Koeppen H., de Sauvage F.J., Davis D.P.
      Cancer Res. 65:9751-9761(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    12. "CDC25B phosphorylated by pEg3 localizes to the centrosome and the spindle poles at mitosis."
      Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P., Monsarrat B., Tassan J.P., Ducommun B.
      Cell Cycle 4:806-811(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25B.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "M-phase MELK activity is regulated by MPF and MAPK."
      Badouel C., Korner R., Frank-Vaillant M., Couturier A., Nigg E.A., Tassan J.P.
      Cell Cycle 5:883-889(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-167; SER-343; SER-356; TYR-367; THR-398; THR-409; SER-431; THR-494; SER-505 AND SER-529.
    15. "Substrate specificity and activity regulation of protein kinase MELK."
      Beullens M., Vancauwenbergh S., Morrice N., Derua R., Ceulemans H., Waelkens E., Bollen M.
      J. Biol. Chem. 280:40003-40011(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, CALCIUM-BINDING, PHOSPHORYLATION AT THR-56; TYR-163; THR-167; SER-171; SER-253; SER-336; SER-343; SER-356; SER-391; THR-398; SER-407; SER-431; THR-494; SER-505; SER-529 AND THR-539, MUTAGENESIS OF CYS-29; CYS-70; CYS-89; ASP-150; CYS-154; TYR-163; CYS-168; CYS-169; SER-171; CYS-204; 283-ASP--ASP-285; CYS-286 AND CYS-339.
    16. "Cell-cycle-dependent cortical localization of pEg3 protein kinase in Xenopus and human cells."
      Chartrain I., Couturier A., Tassan J.P.
      Biol. Cell 98:253-263(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family."
      Lin M.L., Park J.H., Nishidate T., Nakamura Y., Katagiri T.
      Breast Cancer Res. 9:R17-R17(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BCL2L14, MUTAGENESIS OF ASP-150.
    18. "Maternal embryonic leucine zipper kinase transcript abundance correlates with malignancy grade in human astrocytomas."
      Marie S.K., Okamoto O.K., Uno M., Hasegawa A.P., Oba-Shinjo S.M., Cohen T., Camargo A.A., Kosoy A., Carlotti C.G. Jr., Toledo S., Moreira-Filho C.A., Zago M.A., Simpson A.J., Caballero O.L.
      Int. J. Cancer 122:807-815(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    19. Cited for: INVOLVEMENT IN CANCER.
    20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505; THR-518 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 AND SER-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Dysregulated expression of Fau and MELK is associated with poor prognosis in breast cancer."
      Pickard M.R., Green A.R., Ellis I.O., Caldas C., Hedge V.L., Mourtada-Maarabouni M., Williams G.T.
      Breast Cancer Res. 11:R60-R60(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "Maternal embryonic leucine zipper kinase is upregulated and required in mammary tumor-initiating cells in vivo."
      Hebbard L.W., Maurer J., Miller A., Lesperance J., Hassell J., Oshima R.G., Terskikh A.V.
      Cancer Res. 70:8863-8873(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    26. "Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids."
      Moravcevic K., Mendrola J.M., Schmitz K.R., Wang Y.H., Slochower D., Janmey P.A., Lemmon M.A.
      Cell 143:966-977(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    27. "Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit."
      Badouel C., Chartrain I., Blot J., Tassan J.P.
      Exp. Cell Res. 316:2166-2173(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    28. "Resistance of colorectal cancer cells to radiation and 5-FU is associated with MELK expression."
      Choi S., Ku J.L.
      Biochem. Biophys. Res. Commun. 412:207-213(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    29. "Siomycin A targets brain tumor stem cells partially through a MELK-mediated pathway."
      Nakano I., Joshi K., Visnyei K., Hu B., Watanabe M., Lam D., Wexler E., Saigusa K., Nakamura Y., Laks D.R., Mischel P.S., Viapiano M., Kornblum H.I.
      Neuro-oncol. 13:622-634(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    30. "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] MET-56; ARG-219; LYS-333; ILE-348 AND MET-460.

    Entry informationi

    Entry nameiMELK_HUMAN
    AccessioniPrimary (citable) accession number: Q14680
    Secondary accession number(s): A6P3A7
    , A6P3A8, B1AMQ6, B7Z1E6, B7Z5M5, B7Z6Q7, B7Z6R8, B7Z6Y0, B7Z7Q1, D3DRP8, F5H0Y0, F5H2R4, F5H689, Q7L3C3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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

    Potential therapeutic target for treatment of somatic tumors, such as brain and breast cancers, down-regulation of MELK inhibiting tumorigenesis (PubMed:17960622, PubMed:20861186).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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