MELK
entrez
9833
canonical
uniprot
Q14680
canonical
ensembl
ENSG00000165304
resolver
ensp
ENSP00000298048
resolver
ensp
ENSP00000437804
resolver
ensp
ENSP00000439184
resolver
ensp
ENSP00000439792
resolver
ensp
ENSP00000441596
resolver
ensp
ENSP00000443550
resolver
ensp
ENSP00000445452
resolver
ensp
ENSP00000525405
resolver
ensp
ENSP00000525407
resolver
ensp
ENSP00000525408
resolver
ensp
ENSP00000525409
resolver
ensp
ENSP00000525410
resolver
ensp
ENSP00000525412
resolver
ensp
ENSP00000590614
resolver
ensp
ENSP00000590617
resolver
ensp
ENSP00000590618
resolver
ensp
ENSP00000590627
resolver
ensp
ENSP00000590634
resolver
ensp
ENSP00000590637
resolver
genesymbol
MELK
resolver
genesymbol_syn
KIAA0175
resolver
hgnc
HGNC:16870
resolver
uniprot
A6P3A7
resolver
uniprot
A6P3A8
resolver
uniprot
B1AMQ6
resolver
uniprot
B7Z1E6
resolver
uniprot
B7Z1G6
resolver
uniprot
B7Z5M5
resolver
uniprot
B7Z6Q7
resolver
uniprot
B7Z6R8
resolver
uniprot
B7Z6Y0
resolver
uniprot
B7Z7Q1
resolver
uniprot
D3DRP8
resolver
uniprot
F5H0Y0
resolver
uniprot
F5H2R4
resolver
uniprot
F5H689
resolver
uniprot
Q7L3C3
resolver
uniprot_entry
B7Z1G6_HUMAN
resolver
uniprot_entry
MELK_HUMAN
resolver
uniprot_sec
A6P3A7
resolver
uniprot_sec
A6P3A8
resolver
uniprot_sec
B1AMQ6
resolver
uniprot_sec
B7Z1E6
resolver
uniprot_sec
B7Z5M5
resolver
uniprot_sec
B7Z6Q7
resolver
uniprot_sec
B7Z6R8
resolver
uniprot_sec
B7Z6Y0
resolver
uniprot_sec
B7Z7Q1
resolver
uniprot_sec
D3DRP8
resolver
uniprot_sec
F5H0Y0
resolver
uniprot_sec
F5H2R4
resolver
uniprot_sec
F5H689
resolver
uniprot_sec
Q7L3C3
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000269|PubMed:16216881}.
uniprot
proteins
amino_acid_sequence
MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV
uniprot
proteins
disease_involvement
DISEASE: Note=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.
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:11802789, ECO:0000269|PubMed:12400006, ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:15908796, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616}.
uniprot
proteins
mass_dalton
74642
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 70; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 89; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 150; /note="D->A: Abolishes enzymatic activity."; /evidence="ECO:0000269|PubMed:14699119, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:17280616"; MUTAGEN 154; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 163; /note="Y->F: Abolishes autophosphorylation on tyrosine but still active on exogenous substrates."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 167; /note="T->A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 167; /note="T->D,E: Phosphomimetic mutant that has similar kinase activity as wild-type."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 168; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 169; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 171; /note="S->A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 171; /note="S->D: Inactive."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 204; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 283..285; /note="DDD->KKK: Inactive."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 286; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 339; /note="C->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."; /evidence="ECO:0000269|PubMed:16216881"; MUTAGEN 345; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 387; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 409; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 415; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 428; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 446; /note="T->A: Inhibits interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 460; /note="T->A: Inhibits interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 466; /note="T->A: Inhibits interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 478; /note="T->A: Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity."; /evidence="ECO:0000269|PubMed:14699119"; MUTAGEN 518; /note="T->A: No effect on interaction with PPP1R8."; /evidence="ECO:0000269|PubMed:14699119
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000305|PubMed:14699119, ECO:0000305|PubMed:14976552, ECO:0000305|PubMed:16216881, ECO:0000305|PubMed:16628004, ECO:0000305|PubMed:20420823}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SNF1 subfamily
uniprot
proteins
pubmed
11802789
uniprot
proteins
pubmed
12400006
uniprot
proteins
pubmed
14699119
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14976552
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15908796
uniprot
proteins
pubmed
16159311
uniprot
proteins
pubmed
16216881
uniprot
proteins
pubmed
16266996
uniprot
proteins
pubmed
16628004
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17280616
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17722061
uniprot
proteins
pubmed
17960622
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19671159
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20420823
uniprot
proteins
pubmed
20861186
uniprot
proteins
pubmed
21145462
uniprot
proteins
pubmed
21558073
uniprot
proteins
pubmed
21806965
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8724849
uniprot
proteins
sequence_length
651
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16159311, ECO:0000269|PubMed:21145462}; Peripheral membrane protein {ECO:0000269|PubMed:16159311, ECO:0000269|PubMed:21145462}.
uniprot
proteins