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Protein

Maternal embryonic leucine zipper kinase

Gene

MELK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation1 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)DescriptionActionsGraphical viewLength
Binding sitei40ATPPROSITE-ProRule annotation1
Active sitei132Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 25ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: UniProtKB
  • lipid binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • intracellular signal transduction Source: GO_Central
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  • neural precursor cell proliferation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • 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

BioCyciZFISH:HS09215-MONOMER.
SignaLinkiQ14680.
SIGNORiQ14680.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:16870. MELK.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi29C → 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 Publication1
Mutagenesisi70C → 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 Publication1
Mutagenesisi89C → 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 Publication1
Mutagenesisi150D → A: Abolishes enzymatic activity. 3 Publications1
Mutagenesisi154C → 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 Publication1
Mutagenesisi163Y → F: Abolishes autophosphorylation on tyrosine but still active on exogenous substrates. 1 Publication1
Mutagenesisi167T → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. 1 Publication1
Mutagenesisi167T → D or E: Phosphomimetic mutant that has similar kinase activity as wild-type. 1 Publication1
Mutagenesisi168C → 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 Publication1
Mutagenesisi169C → 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 Publication1
Mutagenesisi171S → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. 1 Publication1
Mutagenesisi171S → D: Inactive. 1 Publication1
Mutagenesisi204C → 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 Publication1
Mutagenesisi283 – 285DDD → KKK: Inactive. 1 Publication3
Mutagenesisi286C → 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 Publication1
Mutagenesisi339C → 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 Publication1
Mutagenesisi345T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi387T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi409T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi415T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi428T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi446T → A: Inhibits interaction with PPP1R8. 1 Publication1
Mutagenesisi460T → A: Inhibits interaction with PPP1R8. 1 Publication1
Mutagenesisi466T → A: Inhibits interaction with PPP1R8. 1 Publication1
Mutagenesisi478T → A: Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity. 1 Publication1
Mutagenesisi518T → A: No effect on interaction with PPP1R8. 1 Publication1

Organism-specific databases

DisGeNETi9833.
OpenTargetsiENSG00000165304.
PharmGKBiPA134902874.

Chemistry databases

ChEMBLiCHEMBL4578.
GuidetoPHARMACOLOGYi2102.

Polymorphism and mutation databases

BioMutaiMELK.
DMDMi50400857.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000863231 – 651Maternal embryonic leucine zipper kinaseAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei56Phosphothreonine; by autocatalysis1 Publication1
Modified residuei163Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei167Phosphothreonine; by autocatalysis3 Publications1
Modified residuei171Phosphoserine; by autocatalysis1 Publication1
Modified residuei253Phosphoserine; by autocatalysis1 Publication1
Modified residuei336Phosphoserine; by autocatalysis1 Publication1
Modified residuei343Phosphoserine; by autocatalysis2 Publications1
Modified residuei356Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei367Phosphotyrosine1 Publication1
Modified residuei391Phosphoserine; by autocatalysis1 Publication1
Modified residuei398Phosphothreonine; by autocatalysis2 Publications1
Modified residuei407Phosphoserine; by autocatalysis1 Publication1
Modified residuei409Phosphothreonine1 Publication1
Modified residuei431Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei478Phosphothreonine1 Publication1
Modified residuei494Phosphothreonine; by autocatalysis2 Publications1
Modified residuei498PhosphoserineCombined sources1
Modified residuei505Phosphoserine; by autocatalysisCombined sources2 Publications1
Modified residuei518PhosphothreonineCombined sources1
Modified residuei529PhosphoserineCombined sources2 Publications1
Modified residuei529Phosphoserine; by autocatalysis2 Publications1
Modified residuei539Phosphothreonine; by autocatalysis1 Publication1

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).5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14680.
MaxQBiQ14680.
PaxDbiQ14680.
PeptideAtlasiQ14680.
PRIDEiQ14680.

PTM databases

iPTMnetiQ14680.
PhosphoSitePlusiQ14680.

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

BgeeiENSG00000165304.
CleanExiHS_MELK.
ExpressionAtlasiQ14680. baseline and differential.
GenevisibleiQ14680. HS.

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. 23 interactors.
IntActiQ14680. 3 interactors.
MINTiMINT-7944803.
STRINGi9606.ENSP00000298048.

Chemistry databases

BindingDBiQ14680.

Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Helixi5 – 10Combined sources6
Beta strandi11 – 17Combined sources7
Beta strandi20 – 22Combined sources3
Beta strandi24 – 30Combined sources7
Turni31 – 33Combined sources3
Beta strandi36 – 43Combined sources8
Turni44 – 46Combined sources3
Helixi48 – 50Combined sources3
Helixi52 – 63Combined sources12
Beta strandi72 – 77Combined sources6
Beta strandi79 – 87Combined sources9
Helixi94 – 101Combined sources8
Helixi106 – 125Combined sources20
Helixi135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi146 – 148Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi163 – 166Combined sources4
Helixi172 – 174Combined sources3
Helixi177 – 180Combined sources4
Helixi187 – 204Combined sources18
Helixi214 – 223Combined sources10
Helixi234 – 243Combined sources10
Helixi248 – 250Combined sources3
Helixi254 – 258Combined sources5
Helixi261 – 264Combined sources4
Turni265 – 267Combined sources3
Beta strandi279 – 281Combined sources3
Helixi284 – 291Combined sources8
Beta strandi294 – 296Combined sources3
Helixi298 – 305Combined sources8
Helixi312 – 326Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKYX-ray1.83A2-340[»]
4BKZX-ray2.20A2-340[»]
4BL1X-ray2.60A2-340[»]
4D2PX-ray2.55A/B/C/D1-336[»]
4D2TX-ray2.70A/B/C/D1-336[»]
4D2VX-ray2.45A/B/C/D1-336[»]
4D2WX-ray1.92A/B/C/D1-336[»]
4IXPX-ray2.75A1-340[»]
4UMPX-ray2.30A/B/C/D1-336[»]
4UMQX-ray2.60A1-336[»]
4UMRX-ray3.00A1-336[»]
4UMTX-ray1.98A1-336[»]
4UMUX-ray2.02A1-336[»]
5IH8X-ray1.85A3-330[»]
5IH9X-ray1.79A3-330[»]
5IHAX-ray1.96A3-330[»]
5IHCX-ray2.14A3-330[»]
ProteinModelPortaliQ14680.
SMRiQ14680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 263Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini602 – 651KA1PROSITE-ProRule annotationAdd BLAST50

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni282 – 321UBA-likeAdd BLAST40
Regioni326 – 651Autoinhibitory regionAdd BLAST326

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

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00860000133728.
HOGENOMiHOG000233023.
HOVERGENiHBG106273.
InParanoidiQ14680.
KOiK08799.
OMAiYELHETI.
OrthoDBiEOG091G05V9.
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.
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. AlignAdd to basket

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

        10         20         30         40         50
MKDYDELLKY YELHETIGTG GFAKVKLACH ILTGEMVAIK IMDKNTLGSD
60 70 80 90 100
LPRIKTEIEA LKNLRHQHIC QLYHVLETAN KIFMVLEYCP GGELFDYIIS
110 120 130 140 150
QDRLSEEETR VVFRQIVSAV AYVHSQGYAH RDLKPENLLF DEYHKLKLID
160 170 180 190 200
FGLCAKPKGN KDYHLQTCCG SLAYAAPELI QGKSYLGSEA DVWSMGILLY
210 220 230 240 250
VLMCGFLPFD DDNVMALYKK IMRGKYDVPK WLSPSSILLL QQMLQVDPKK
260 270 280 290 300
RISMKNLLNH PWIMQDYNYP VEWQSKNPFI HLDDDCVTEL SVHHRNNRQT
310 320 330 340 350
MEDLISLWQY DHLTATYLLL LAKKARGKPV RLRLSSFSCG QASATPFTDI
360 370 380 390 400
KSNNWSLEDV TASDKNYVAG LIDYDWCEDD LSTGAATPRT SQFTKYWTES
410 420 430 440 450
NGVESKSLTP ALCRTPANKL KNKENVYTPK SAVKNEEYFM FPEPKTPVNK
460 470 480 490 500
NQHKREILTT PNRYTTPSKA RNQCLKETPI KIPVNSTGTD KLMTGVISPE
510 520 530 540 550
RRCRSVELDL NQAHMEETPK RKGAKVFGSL ERGLDKVITV LTRSKRKGSA
560 570 580 590 600
RDGPRRLKLH YNVTTTRLVN PDQLLNEIMS ILPKKHVDFV QKGYTLKCQT
610 620 630 640 650
QSDFGKVTMQ FELEVCQLQK PDVVGIRRQR LKGDAWVYKR LVEDILSSCK

V
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69I → M in BAH12961 (PubMed:14702039).Curated1
Sequence conflicti398T → A in BAH12961 (PubMed:14702039).Curated1
Sequence conflicti428T → A in BAH11482 (PubMed:14702039).Curated1
Sequence conflicti474C → R in BAH13343 (PubMed:14702039).Curated1
Sequence conflicti483P → L in BAH13354 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04079456T → M.1 PublicationCorresponds to variant rs35233455dbSNPEnsembl.1
Natural variantiVAR_040795219K → R.1 PublicationCorresponds to variant rs35142210dbSNPEnsembl.1
Natural variantiVAR_040796333R → K.1 PublicationCorresponds to variant rs34655121dbSNPEnsembl.1
Natural variantiVAR_040797348T → I.1 PublicationCorresponds to variant rs55845414dbSNPEnsembl.1
Natural variantiVAR_040798460T → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs144052967dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0452081 – 194Missing in isoform 3. 1 PublicationAdd BLAST194
Alternative sequenceiVSP_0452091 – 135MKDYD…RDLKP → MVLE in isoform 4. 1 PublicationAdd BLAST135
Alternative sequenceiVSP_0454301 – 87MKDYD…FMVLE → MMNFSNIMNYMKLLGQ in isoform 5. 2 PublicationsAdd BLAST87
Alternative sequenceiVSP_0454311 – 48MKDYD…KNTLG → MMNFSNIMNYMKLLGQ in isoform 6. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_04471588 – 158Missing in isoform 2. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_04675988 – 135Missing in isoform 8. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_046760352 – 392Missing in isoform 7. 1 PublicationAdd BLAST41

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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]
XP_011516378.1. XM_011518076.2. [Q14680-1]
XP_011516379.1. XM_011518077.1. [Q14680-1]
XP_011516380.1. XM_011518078.2. [Q14680-1]
XP_011516381.1. XM_011518079.1. [Q14680-1]
XP_011516383.1. XM_011518081.2. [Q14680-6]
XP_011516384.1. XM_011518082.2. [Q14680-6]
XP_011516385.1. XM_011518083.2. [Q14680-6]
XP_011516386.1. XM_011518084.2. [Q14680-6]
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.5. human. [Q14680-1]

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:
EMBLi
GenBanki
DDBJi
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]
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]
XP_011516378.1. XM_011518076.2. [Q14680-1]
XP_011516379.1. XM_011518077.1. [Q14680-1]
XP_011516380.1. XM_011518078.2. [Q14680-1]
XP_011516381.1. XM_011518079.1. [Q14680-1]
XP_011516383.1. XM_011518081.2. [Q14680-6]
XP_011516384.1. XM_011518082.2. [Q14680-6]
XP_011516385.1. XM_011518083.2. [Q14680-6]
XP_011516386.1. XM_011518084.2. [Q14680-6]
UniGeneiHs.184339.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKYX-ray1.83A2-340[»]
4BKZX-ray2.20A2-340[»]
4BL1X-ray2.60A2-340[»]
4D2PX-ray2.55A/B/C/D1-336[»]
4D2TX-ray2.70A/B/C/D1-336[»]
4D2VX-ray2.45A/B/C/D1-336[»]
4D2WX-ray1.92A/B/C/D1-336[»]
4IXPX-ray2.75A1-340[»]
4UMPX-ray2.30A/B/C/D1-336[»]
4UMQX-ray2.60A1-336[»]
4UMRX-ray3.00A1-336[»]
4UMTX-ray1.98A1-336[»]
4UMUX-ray2.02A1-336[»]
5IH8X-ray1.85A3-330[»]
5IH9X-ray1.79A3-330[»]
5IHAX-ray1.96A3-330[»]
5IHCX-ray2.14A3-330[»]
ProteinModelPortaliQ14680.
SMRiQ14680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115171. 23 interactors.
IntActiQ14680. 3 interactors.
MINTiMINT-7944803.
STRINGi9606.ENSP00000298048.

Chemistry databases

BindingDBiQ14680.
ChEMBLiCHEMBL4578.
GuidetoPHARMACOLOGYi2102.

PTM databases

iPTMnetiQ14680.
PhosphoSitePlusiQ14680.

Polymorphism and mutation databases

BioMutaiMELK.
DMDMi50400857.

Proteomic databases

EPDiQ14680.
MaxQBiQ14680.
PaxDbiQ14680.
PeptideAtlasiQ14680.
PRIDEiQ14680.

Protocols and materials databases

DNASUi9833.
Structural Biology KnowledgebaseSearch...

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.5. human. [Q14680-1]

Organism-specific databases

CTDi9833.
DisGeNETi9833.
GeneCardsiMELK.
HGNCiHGNC:16870. MELK.
HPAiHPA017214.
MIMi607025. gene.
neXtProtiNX_Q14680.
OpenTargetsiENSG00000165304.
PharmGKBiPA134902874.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00860000133728.
HOGENOMiHOG000233023.
HOVERGENiHBG106273.
InParanoidiQ14680.
KOiK08799.
OMAiYELHETI.
OrthoDBiEOG091G05V9.
PhylomeDBiQ14680.
TreeFamiTF314032.

Enzyme and pathway databases

BioCyciZFISH:HS09215-MONOMER.
SignaLinkiQ14680.
SIGNORiQ14680.

Miscellaneous databases

ChiTaRSiMELK. human.
GeneWikiiMELK.
GenomeRNAii9833.
PROiQ14680.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165304.
CleanExiHS_MELK.
ExpressionAtlasiQ14680. baseline and differential.
GenevisibleiQ14680. HS.

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.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.