Q14680 (MELK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Maternal embryonic leucine zipper kinase
Short name=hMELK
EC=2.7.11.1

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 names

Name:	MELK
Synonyms:	KIAA0175

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	651 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.9 Ref.12 Ref.15 Ref.17
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.15 ATP + a protein = ADP + a phosphoprotein. Ref.15
Enzyme 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. Ref.15
Subunit structure	Monomer. Interacts with ZNF622 and PPP1R8. Ref.7 Ref.9
Subcellular location	Cell membrane; Peripheral membrane protein Ref.16 Ref.26.
Tissue specificity	Expressed in placenta, kidney, thymus, testis, ovary and intestine. Ref.2
Developmental stage	Increases during G2/M phase compared to interphase. Protein level decreases when cells exit mitosis, probably due to degradation. Ref.27
Induction	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. Ref.15 Ref.28 Ref.29
Domain	The KA1 domain mediates binding to phospholipids and targeting to membranes By similarity.
Post-translational modification	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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.27
Involvement in disease	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.
Miscellaneous	Potential therapeutic target for treatment of somatic tumors, such as brain and breast cancers, down-regulation of MELK inhibiting tumorigenesis (Ref.18, Ref.25).
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 KA1 (kinase-associated) domain. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA11492.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Calcium Lipid-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement Ref.8. Source: UniProtKB apoptotic process Inferred from direct assay Ref.17. Source: UniProtKB hemopoiesis Inferred from sequence or structural similarity. Source: UniProtKB neural precursor cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.15. Source: UniProtKB
Cellular_component	cell cortex Inferred from direct assay Ref.16. Source: UniProtKB plasma membrane Inferred from direct assay Ref.26. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from direct assay Ref.15. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from direct assay Ref.15. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.8Ref.12Ref.15Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2L14	Q9BZR8	4	EBI-1046702,EBI-1385773

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14680-1)

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.

Isoform 2 (identifier: Q14680-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q14680-3)

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

Isoform 4 (identifier: Q14680-4)

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

Isoform 5 (identifier: Q14680-5)

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

Isoform 6 (identifier: Q14680-6)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 651

651

Maternal embryonic leucine zipper kinase

PRO_0000086323

Regions

Domain

11 – 263

253

Protein kinase

Domain

602 – 651

50

KA1

Nucleotide binding

17 – 25

9

ATP By similarity

Region

282 – 321

40

UBA-like

Region

326 – 651

326

Autoinhibitory region

Sites

Active site

132

1

Proton acceptor By similarity

Binding site

40

1

ATP By similarity

Amino acid modifications

Modified residue

56

1

Phosphothreonine; by autocatalysis Ref.15

Modified residue

163

1

Phosphotyrosine; by autocatalysis Ref.15

Modified residue

167

1

Phosphothreonine; by autocatalysis Ref.10 Ref.14 Ref.15

Modified residue

171

1

Phosphoserine; by autocatalysis Ref.15

Modified residue

253

1

Phosphoserine; by autocatalysis Ref.15

Modified residue

336

1

Phosphoserine; by autocatalysis Ref.15

Modified residue

343

1

Phosphoserine; by autocatalysis Ref.14 Ref.15

Modified residue

356

1

Phosphoserine; by autocatalysis Ref.14 Ref.15 Ref.20 Ref.23 Ref.24

Modified residue

367

1

Phosphotyrosine Ref.14

Modified residue

391

1

Phosphoserine; by autocatalysis Ref.15

Modified residue

398

1

Phosphothreonine; by autocatalysis Ref.14 Ref.15

Modified residue

407

1

Phosphoserine; by autocatalysis Ref.15

Modified residue

409

1

Phosphothreonine Ref.14

Modified residue

431

1

Phosphoserine; by autocatalysis Ref.14 Ref.15 Ref.21

Modified residue

478

1

Phosphothreonine Ref.9

Modified residue

494

1

Phosphothreonine; by autocatalysis Ref.14 Ref.15

Modified residue

498

1

Phosphoserine Ref.20 Ref.23

Modified residue

505

1

Phosphoserine; by autocatalysis Ref.13 Ref.14 Ref.15 Ref.20 Ref.21 Ref.23

Modified residue

518

1

Phosphothreonine Ref.20

Modified residue

529

1

Phosphoserine; alternate Ref.14 Ref.15 Ref.20 Ref.23

Modified residue

529

1

Phosphoserine; by autocatalysis; alternate Ref.14 Ref.15 Ref.20 Ref.23

Modified residue

539

1

Phosphothreonine; by autocatalysis Ref.15

Natural variations

Alternative sequence

1 – 194

194

Missing in isoform 3.

VSP_045208

Alternative sequence

1 – 135

135

MKDYD…RDLKP → MVLE in isoform 4.

VSP_045209

Alternative sequence

1 – 87

87

MKDYD…FMVLE → MMNFSNIMNYMKLLGQ in isoform 5.

VSP_045430

Alternative sequence

1 – 48

48

MKDYD…KNTLG → MMNFSNIMNYMKLLGQ in isoform 6.

VSP_045431

Alternative sequence

88 – 158

71

Missing in isoform 2.

VSP_044715

Natural variant

56

1

T → M. Ref.30
Corresponds to variant rs35233455 [ dbSNP | Ensembl ].

VAR_040794

Natural variant

219

1

K → R. Ref.30
Corresponds to variant rs35142210 [ dbSNP | Ensembl ].

VAR_040795

Natural variant

333

1

R → K. Ref.30
Corresponds to variant rs34655121 [ dbSNP | Ensembl ].

VAR_040796

Natural variant

348

1

T → I. Ref.30
Corresponds to variant rs55845414 [ dbSNP | Ensembl ].

VAR_040797

Natural variant

460

1

T → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.30

VAR_040798

Experimental info

Mutagenesis

29

1

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. Ref.15

Mutagenesis

70

1

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. Ref.15

Mutagenesis

89

1

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. Ref.15

Mutagenesis

150

1

D → A: Abolishes enzymatic activity. Ref.9 Ref.15 Ref.17

Mutagenesis

154

1

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. Ref.15

Mutagenesis

163

1

Y → F: Abolishes autophosphorylation on tyrosine but still active on exogenous substrates. Ref.15

Mutagenesis

167

1

T → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. Ref.10

Mutagenesis

167

1

T → D or E: Phosphomimetic mutant that has similar kinase activity as wild-type. Ref.10

Mutagenesis

168

1

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. Ref.15

Mutagenesis

169

1

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. Ref.15

Mutagenesis

171

1

S → A: Abolishes activation of serine/threonine-protein kinase activity and has only weak activity. Ref.15

Mutagenesis

171

1

S → D: Inactive. Ref.15

Mutagenesis

204

1

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. Ref.15

Mutagenesis

283 – 285

3

DDD → KKK: Inactive. Ref.15

Mutagenesis

286

1

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. Ref.15

Mutagenesis

339

1

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. Ref.15

Mutagenesis

345

1

T → A: No effect on interaction with PPP1R8. Ref.9

Mutagenesis

387

1

T → A: No effect on interaction with PPP1R8. Ref.9

Mutagenesis

409

1

T → A: No effect on interaction with PPP1R8. Ref.9

Mutagenesis

415

1

T → A: No effect on interaction with PPP1R8. Ref.9

Mutagenesis

428

1

T → A: No effect on interaction with PPP1R8. Ref.9

Mutagenesis

446

1

T → A: Inhibits interaction with PPP1R8. Ref.9

Mutagenesis

460

1

T → A: Inhibits interaction with PPP1R8. Ref.9

Mutagenesis

466

1

T → A: Inhibits interaction with PPP1R8. Ref.9

Mutagenesis

478

1

T → A: Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity. Ref.9

Mutagenesis

518

1

T → A: No effect on interaction with PPP1R8. Ref.9

Sequence conflict

428

1

T → A in BAH11482. Ref.3

Sequence conflict

483

1

P → L in BAH13354. Ref.3

Secondary structure

1

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651

Helix Strand Turn

Details...

Turn

5 – 10

6

Beta strand

11 – 19

9

Beta strand

24 – 30

7

Turn

31 – 33

3

Beta strand

36 – 45

10

Helix

53 – 62

10

Beta strand

72 – 77

6

Beta strand

79 – 87

9

Helix

94 – 101

8

Helix

106 – 125

20

Helix

135 – 137

3

Beta strand

138 – 140

3

Beta strand

146 – 148

3

Helix

172 – 174

3

Helix

177 – 180

4

Helix

189 – 204

16

Helix

214 – 223

10

Helix

234 – 243

10

Helix

248 – 250

3

Helix

254 – 258

5

Helix

261 – 264

4

Turn

265 – 267

3

Helix

284 – 293

10

Helix

298 – 305

8

Helix

312 – 325

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2004. Version 3. Checksum: 57F05CDC6122E570	FASTA	651	74,642
	10 20 30 40 50 60 MKDYDELLKY YELHETIGTG GFAKVKLACH ILTGEMVAIK IMDKNTLGSD LPRIKTEIEA 70 80 90 100 110 120 LKNLRHQHIC QLYHVLETAN KIFMVLEYCP GGELFDYIIS QDRLSEEETR VVFRQIVSAV 130 140 150 160 170 180 AYVHSQGYAH RDLKPENLLF DEYHKLKLID FGLCAKPKGN KDYHLQTCCG SLAYAAPELI 190 200 210 220 230 240 QGKSYLGSEA DVWSMGILLY VLMCGFLPFD DDNVMALYKK IMRGKYDVPK WLSPSSILLL 250 260 270 280 290 300 QQMLQVDPKK RISMKNLLNH PWIMQDYNYP VEWQSKNPFI HLDDDCVTEL SVHHRNNRQT 310 320 330 340 350 360 MEDLISLWQY DHLTATYLLL LAKKARGKPV RLRLSSFSCG QASATPFTDI KSNNWSLEDV 370 380 390 400 410 420 TASDKNYVAG LIDYDWCEDD LSTGAATPRT SQFTKYWTES NGVESKSLTP ALCRTPANKL 430 440 450 460 470 480 KNKENVYTPK SAVKNEEYFM FPEPKTPVNK NQHKREILTT PNRYTTPSKA RNQCLKETPI 490 500 510 520 530 540 KIPVNSTGTD KLMTGVISPE RRCRSVELDL NQAHMEETPK RKGAKVFGSL ERGLDKVITV 550 560 570 580 590 600 LTRSKRKGSA RDGPRRLKLH YNVTTTRLVN PDQLLNEIMS ILPKKHVDFV QKGYTLKCQT 610 620 630 640 650 QSDFGKVTMQ FELEVCQLQK PDVVGIRRQR LKGDAWVYKR LVEDILSSCK V
	Isoform 2 [UniParc]. Checksum: B91D7CA0BA90C2C1	FASTA	580	66,399
	10 20 30 40 50 60 MKDYDELLKY YELHETIGTG GFAKVKLACH ILTGEMVAIK IMDKNTLGSD LPRIKTEIEA 70 80 90 100 110 120 LKNLRHQHIC QLYHVLETAN KIFMVLEGNK DYHLQTCCGS LAYAAPELIQ GKSYLGSEAD 130 140 150 160 170 180 VWSMGILLYV LMCGFLPFDD DNVMALYKKI MRGKYDVPKW LSPSSILLLQ QMLQVDPKKR 190 200 210 220 230 240 ISMKNLLNHP WIMQDYNYPV EWQSKNPFIH LDDDCVTELS VHHRNNRQTM EDLISLWQYD 250 260 270 280 290 300 HLTATYLLLL AKKARGKPVR LRLSSFSCGQ ASATPFTDIK SNNWSLEDVT ASDKNYVAGL 310 320 330 340 350 360 IDYDWCEDDL STGAATPRTS QFTKYWTESN GVESKSLTPA LCRTPANKLK NKENVYTPKS 370 380 390 400 410 420 AVKNEEYFMF PEPKTPVNKN QHKREILTTP NRYTTPSKAR NQCLKETPIK IPVNSTGTDK 430 440 450 460 470 480 LMTGVISPER RCRSVELDLN QAHMEETPKR KGAKVFGSLE RGLDKVITVL TRSKRKGSAR 490 500 510 520 530 540 DGPRRLKLHY NVTTTRLVNP DQLLNEIMSI LPKKHVDFVQ KGYTLKCQTQ SDFGKVTMQF 550 560 570 580 ELEVCQLQKP DVVGIRRQRL KGDAWVYKRL VEDILSSCKV
	Isoform 3 [UniParc]. Checksum: 8E6CB0758D50AC49	FASTA	457	52,528
	10 20 30 40 50 60 MGILLYVLMC GFLPFDDDNV MALYKKIMRG KYDVPKWLSP SSILLLQQML QVDPKKRISM 70 80 90 100 110 120 KNLLNHPWIM QDYNYPVEWQ SKNPFIHLDD DCVTELSVHH RNNRQTMEDL ISLWQYDHLT 130 140 150 160 170 180 ATYLLLLAKK ARGKPVRLRL SSFSCGQASA TPFTDIKSNN WSLEDVTASD KNYVAGLIDY 190 200 210 220 230 240 DWCEDDLSTG AATPRTSQFT KYWTESNGVE SKSLTPALCR TPANKLKNKE NVYTPKSAVK 250 260 270 280 290 300 NEEYFMFPEP KTPVNKNQHK REILTTPNRY TTPSKARNQC LKETPIKIPV NSTGTDKLMT 310 320 330 340 350 360 GVISPERRCR SVELDLNQAH MEETPKRKGA KVFGSLERGL DKVITVLTRS KRKGSARDGP 370 380 390 400 410 420 RRLKLHYNVT TTRLVNPDQL LNEIMSILPK KHVDFVQKGY TLKCQTQSDF GKVTMQFELE 430 440 450 VCQLQKPDVV GIRRQRLKGD AWVYKRLVED ILSSCKV
	Isoform 4 [UniParc]. Checksum: F56647A88C371BBF	FASTA	520	59,576
	10 20 30 40 50 60 MVLEENLLFD EYHKLKLIDF GLCAKPKGNK DYHLQTCCGS LAYAAPELIQ GKSYLGSEAD 70 80 90 100 110 120 VWSMGILLYV LMCGFLPFDD DNVMALYKKI MRGKYDVPKW LSPSSILLLQ QMLQVDPKKR 130 140 150 160 170 180 ISMKNLLNHP WIMQDYNYPV EWQSKNPFIH LDDDCVTELS VHHRNNRQTM EDLISLWQYD 190 200 210 220 230 240 HLTATYLLLL AKKARGKPVR LRLSSFSCGQ ASATPFTDIK SNNWSLEDVT ASDKNYVAGL 250 260 270 280 290 300 IDYDWCEDDL STGAATPRTS QFTKYWTESN GVESKSLTPA LCRTPANKLK NKENVYTPKS 310 320 330 340 350 360 AVKNEEYFMF PEPKTPVNKN QHKREILTTP NRYTTPSKAR NQCLKETPIK IPVNSTGTDK 370 380 390 400 410 420 LMTGVISPER RCRSVELDLN QAHMEETPKR KGAKVFGSLE RGLDKVITVL TRSKRKGSAR 430 440 450 460 470 480 DGPRRLKLHY NVTTTRLVNP DQLLNEIMSI LPKKHVDFVQ KGYTLKCQTQ SDFGKVTMQF 490 500 510 520 ELEVCQLQKP DVVGIRRQRL KGDAWVYKRL VEDILSSCKV
	Isoform 5 [UniParc]. Checksum: 1A6547694E09401B	FASTA	580	66,547
	10 20 30 40 50 60 MMNFSNIMNY MKLLGQYCPG GELFDYIISQ DRLSEEETRV VFRQIVSAVA YVHSQGYAHR 70 80 90 100 110 120 DLKPENLLFD EYHKLKLIDF GLCAKPKGNK DYHLQTCCGS LAYAAPELIQ GKSYLGSEAD 130 140 150 160 170 180 VWSMGILLYV LMCGFLPFDD DNVMALYKKI MRGKYDVPKW LSPSSILLLQ QMLQVDPKKR 190 200 210 220 230 240 ISMKNLLNHP WIMQDYNYPV EWQSKNPFIH LDDDCVTELS VHHRNNRQTM EDLISLWQYD 250 260 270 280 290 300 HLTATYLLLL AKKARGKPVR LRLSSFSCGQ ASATPFTDIK SNNWSLEDVT ASDKNYVAGL 310 320 330 340 350 360 IDYDWCEDDL STGAATPRTS QFTKYWTESN GVESKSLTPA LCRTPANKLK NKENVYTPKS 370 380 390 400 410 420 AVKNEEYFMF PEPKTPVNKN QHKREILTTP NRYTTPSKAR NQCLKETPIK IPVNSTGTDK 430 440 450 460 470 480 LMTGVISPER RCRSVELDLN QAHMEETPKR KGAKVFGSLE RGLDKVITVL TRSKRKGSAR 490 500 510 520 530 540 DGPRRLKLHY NVTTTRLVNP DQLLNEIMSI LPKKHVDFVQ KGYTLKCQTQ SDFGKVTMQF 550 560 570 580 ELEVCQLQKP DVVGIRRQRL KGDAWVYKRL VEDILSSCKV
	Isoform 6 [UniParc]. Checksum: AF6938BF6FFB3CE4	FASTA	619	71,174
	10 20 30 40 50 60 MMNFSNIMNY MKLLGQSDLP RIKTEIEALK NLRHQHICQL YHVLETANKI FMVLEYCPGG 70 80 90 100 110 120 ELFDYIISQD RLSEEETRVV FRQIVSAVAY VHSQGYAHRD LKPENLLFDE YHKLKLIDFG 130 140 150 160 170 180 LCAKPKGNKD YHLQTCCGSL AYAAPELIQG KSYLGSEADV WSMGILLYVL MCGFLPFDDD 190 200 210 220 230 240 NVMALYKKIM RGKYDVPKWL SPSSILLLQQ MLQVDPKKRI SMKNLLNHPW IMQDYNYPVE 250 260 270 280 290 300 WQSKNPFIHL DDDCVTELSV HHRNNRQTME DLISLWQYDH LTATYLLLLA KKARGKPVRL 310 320 330 340 350 360 RLSSFSCGQA SATPFTDIKS NNWSLEDVTA SDKNYVAGLI DYDWCEDDLS TGAATPRTSQ 370 380 390 400 410 420 FTKYWTESNG VESKSLTPAL CRTPANKLKN KENVYTPKSA VKNEEYFMFP EPKTPVNKNQ 430 440 450 460 470 480 HKREILTTPN RYTTPSKARN QCLKETPIKI PVNSTGTDKL MTGVISPERR CRSVELDLNQ 490 500 510 520 530 540 AHMEETPKRK GAKVFGSLER GLDKVITVLT RSKRKGSARD GPRRLKLHYN VTTTRLVNPD 550 560 570 580 590 600 QLLNEIMSIL PKKHVDFVQK GYTLKCQTQS DFGKVTMQFE LEVCQLQKPD VVGIRRQRLK 610 GDAWVYKRLV EDILSSCKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 AND 5). 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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]	"Maternal embryonic leucine zipper kinase is a key regulator of the proliferation of malignant brain tumors, including brain tumor stem cells." Nakano I., Masterman-Smith M., Saigusa K., Paucar A.A., Horvath S., Shoemaker L., Watanabe M., Negro A., Bajpai R., Howes A., Lelievre V., Waschek J.A., Lazareff J.A., Freije W.A., Liau L.M., Gilbertson R.J., Cloughesy T.F., Geschwind D.H. , Nelson S.F., Mischel P.S., Terskikh A.V., Kornblum H.I. J. Neurosci. Res. 86:48-60(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 AND SER-505, MASS SPECTROMETRY. 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-498; SER-505 AND SER-529, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.

IPI

IPI00006471.
IPI01018865.

RefSeq

NP_001243614.1. NM_001256685.1.
NP_001243616.1. NM_001256687.1.
NP_001243617.1. NM_001256688.1.
NP_001243618.1. NM_001256689.1.
NP_001243619.1. NM_001256690.1.
NP_001243621.1. NM_001256692.1.
NP_001243622.1. NM_001256693.1.
NP_055606.1. NM_014791.3.

UniGene

Hs.184339.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZGW	X-ray	2.60	A	2-340	[»]

ProteinModelPortal

Q14680.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14680. 2 interactions.

STRING

9606.ENSP00000298048.

PTM databases

PhosphoSite

Q14680.

Polymorphism databases

DMDM

50400857.

Proteomic databases

PaxDb

Q14680.

PRIDE

Q14680.

Protocols and materials databases

DNASU

9833.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000298048; ENSP00000298048; ENSG00000165304.
ENST00000536329; ENSP00000443550; ENSG00000165304.
ENST00000536987; ENSP00000439184; ENSG00000165304.
ENST00000538311; ENSP00000438226; ENSG00000165304.
ENST00000543751; ENSP00000441596; ENSG00000165304.
ENST00000545008; ENSP00000445452; ENSG00000165304.

GeneID

9833.

KEGG

hsa:9833.

UCSC

uc003zzn.3. human.

Organism-specific databases

CTD

9833.

GeneCards

GC09P036562.

HGNC

HGNC:16870. MELK.

HPA

HPA017214.

MIM

607025. gene.

neXtProt

NX_Q14680.

PharmGKB

PA134902874.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233023.

HOVERGEN

HBG106273.

InParanoid

Q14680.

KO

K08799.

OMA

VCQLQKP.

OrthoDB

EOG4BCDMQ.

PhylomeDB

Q14680.

Gene expression databases

ArrayExpress

Q14680.

Bgee

Q14680.

CleanEx

HS_MELK.

Genevestigator

Q14680.

GermOnline

ENSG00000165304. Homo sapiens.

Family and domain databases

InterPro

IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF103243. Kinase-assoc_KA1. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q14680.

ChEMBL

CHEMBL4578.

GenomeRNAi

9833.

NextBio

35480044.

SOURCE

Search...

Entry information

Entry name

MELK_HUMAN

Accession

Primary (citable) accession number: Q14680
Secondary accession number(s): A6P3A7 , A6P3A8, B1AMQ6, B7Z1E6, B7Z6R8, B7Z6Y0, B7Z7Q1, D3DRP8, F5H2R4, Q7L3C3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.