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Q14680

- MELK_HUMAN

UniProt

Q14680 - MELK_HUMAN

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Protein

Maternal embryonic leucine zipper kinase

Gene
MELK, KIAA0175
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication
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 – 401ATP By similarity
Active sitei132 – 1321Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 259ATP By similarity

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
Complete GO annotation...

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; Peripheral membrane protein 2 Publications

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

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. 1 Publication
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 autocatalysis1 Publication
Modified residuei163 – 1631Phosphotyrosine; by autocatalysis1 Publication
Modified residuei167 – 1671Phosphothreonine; by autocatalysis3 Publications
Modified residuei171 – 1711Phosphoserine; by autocatalysis1 Publication
Modified residuei253 – 2531Phosphoserine; by autocatalysis1 Publication
Modified residuei336 – 3361Phosphoserine; by autocatalysis1 Publication
Modified residuei343 – 3431Phosphoserine; by autocatalysis2 Publications
Modified residuei356 – 3561Phosphoserine; by autocatalysis5 Publications
Modified residuei367 – 3671Phosphotyrosine1 Publication
Modified residuei391 – 3911Phosphoserine; by autocatalysis1 Publication
Modified residuei398 – 3981Phosphothreonine; by autocatalysis2 Publications
Modified residuei407 – 4071Phosphoserine; by autocatalysis1 Publication
Modified residuei409 – 4091Phosphothreonine1 Publication
Modified residuei431 – 4311Phosphoserine; by autocatalysis3 Publications
Modified residuei478 – 4781Phosphothreonine1 Publication
Modified residuei494 – 4941Phosphothreonine; by autocatalysis2 Publications
Modified residuei498 – 4981Phosphoserine2 Publications
Modified residuei505 – 5051Phosphoserine; by autocatalysis6 Publications
Modified residuei518 – 5181Phosphothreonine1 Publication
Modified residuei529 – 5291Phosphoserine; alternate4 Publications
Modified residuei529 – 5291Phosphoserine; by autocatalysis; alternate4 Publications
Modified residuei539 – 5391Phosphothreonine; by autocatalysis1 Publication

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 Inferred.5 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.3 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 263253Protein kinaseAdd
BLAST
Domaini602 – 65150KA1Add
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

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.

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. VSP_045208Add
BLAST
Alternative sequencei1 – 135135MKDYD…RDLKP → MVLE in isoform 4. VSP_045209Add
BLAST
Alternative sequencei1 – 8787MKDYD…FMVLE → MMNFSNIMNYMKLLGQ in isoform 5. VSP_045430Add
BLAST
Alternative sequencei1 – 4848MKDYD…KNTLG → MMNFSNIMNYMKLLGQ in isoform 6. VSP_045431Add
BLAST
Alternative sequencei88 – 15871Missing in isoform 2. VSP_044715Add
BLAST
Alternative sequencei88 – 13548Missing in isoform 8. VSP_046759Add
BLAST
Alternative sequencei352 – 39241Missing in isoform 7. VSP_046760Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691I → M in BAH12961. 1 Publication
Sequence conflicti398 – 3981T → A in BAH12961. 1 Publication
Sequence conflicti428 – 4281T → A in BAH11482. 1 Publication
Sequence conflicti474 – 4741C → R in BAH13343. 1 Publication
Sequence conflicti483 – 4831P → L in BAH13354. 1 Publication

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]
ENST00000538311; ENSP00000438226; ENSG00000165304. [Q14680-3]
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 ]
ENST00000538311 ; ENSP00000438226 ; ENSG00000165304 . [Q14680-3 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 136 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 (1 Publication, 1 Publication).

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

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