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Protein Page:
MELK (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MELK 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. Monomer. Interacts with ZNF622 and PPP1R8. 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. Expressed in placenta, kidney, thymus, testis, ovary and intestine. 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. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, CAMK; Kinase, protein; EC 2.7.11.1; RNA splicing; Protein kinase, Ser/Thr (non-receptor); EC 2.7.10.2; CAMK group; CAMKL family; MELK subfamily
Cellular Component: membrane; plasma membrane; cell cortex
Molecular Function: protein serine/threonine kinase activity; protein binding; non-membrane spanning protein tyrosine kinase activity; calcium ion binding; lipid binding; ATP binding
Biological Process: cell proliferation; peptidyl-tyrosine phosphorylation; positive regulation of apoptosis; apoptosis; protein amino acid autophosphorylation; hemopoiesis; G2/M transition of mitotic cell cycle; induction of apoptosis by oxidative stress
Reference #:  Q14680 (UniProtKB)
Alt. Names/Synonyms: hMELK; hPK38; KIAA0175; Maternal embryonic leucine zipper kinase; MELK; pEg3 kinase; Protein kinase PK38
Gene Symbols: MELK
Molecular weight: 74,642 Da
Basal Isoelectric point: 8.92  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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MELK

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
translation, altered: T478‑p
enzymatic activity, induced: T167‑p, S171‑p
molecular association, regulation: T478‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 5 Y4-p ____MKDyDELLKYY
0 1 K44-ub VAIKIMDkNTLGsDL
0 1 S49-p MDkNTLGsDLPRIkt
0 1 K55-ub GsDLPRIktEIEALk
1 0 T56-p sDLPRIktEIEALkN
0 1 K62-ub ktEIEALkNLRHQHI
0 1 K134-ub GYAHRDLkPENLLFD
0 1 K145-ub LLFDEYHkLKLIDFG
1 0 Y163-p KPKGNKDyHLQtCCG
2 1 T167-p NKDyHLQtCCGsLAY
1 0 S171-p HLQtCCGsLAYAAPE
0 1 S236-p PKWLSPSsILLLQQM
1 0 S253-p VDPKKRIsMKNLLNH
0 6 Y267-p HPWIMQDyNyPVEWQ
0 4 Y269-p WIMQDyNyPVEWQSK
0 15 S335-p KPVRLRLssFsCGQA
1 15 S336-p PVRLRLssFsCGQAs
0 2 S338-p RLRLssFsCGQAsAt
1 2 S343-p sFsCGQAsAtPFtDI
0 3 T345-p sCGQAsAtPFtDIKS
0 1 T348-p QAsAtPFtDIKSNNW
1 15 S356-p DIKSNNWsLEDVTAs
0 1 T361 NWsLEDVTAsDKNyV
0 1 A362 WsLEDVTAsDKNyVA
0 2 S363-p sLEDVTAsDKNyVAG
0 1 Y367-p VTAsDKNyVAGLIDY
0 1 Y374 yVAGLIDYDWCEDDL
0 1 T387-p DLSTGAAtPRTsQFT
1 0 S391-p GAAtPRTsQFTkYWt
0 2 K395-ub PRTsQFTkYWtEsNG
1 1 T398-p sQFTkYWtEsNGVEs
0 1 S400-p FTkYWtEsNGVEsKs
0 1 S405-p tEsNGVEsKsLtPAL
1 2 S407-p sNGVEsKsLtPALCR
0 3 T409-p GVEsKsLtPALCRtP
0 3 T415-p LtPALCRtPANKLKN
0 29 Y427-p LKNKENVytPKsAVk
0 4 T428-p KNKENVytPKsAVkN
1 4 S431-p ENVytPKsAVkNEEy
0 1 A432 NVytPKsAVkNEEyF
0 1 K434-ub ytPKsAVkNEEyFMF
0 209 Y438-p sAVkNEEyFMFPEPK
0 37 T446-p FMFPEPKtPVNKNQH
0 4 T459-p QHKREILttPNRYTt
0 8 T460-p HKREILttPNRYTtP
0 1 N462 REILttPNRYTtPsK
0 2 T466-p ttPNRYTtPsKARNQ
0 1 S468-p PNRYTtPsKARNQCL
1 8 T478-p RNQCLKEtPIkIPVN
0 1 K481-ub CLKEtPIkIPVNsTG
0 1 S486-p PIkIPVNsTGtDkLM
0 1 T489-p IPVNsTGtDkLMtGV
0 1 K491-ub VNsTGtDkLMtGVIs
1 3 T494-p TGtDkLMtGVIsPER
0 13 S498-p kLMtGVIsPERRCRs
1 18 S505-p sPERRCRsVELDLNQ
0 4 T518-p NQAHMEEtPKRKGAK
1 30 S529-p KGAKVFGsLERGLDk
0 1 K536-ub sLERGLDkVItVLtR
1 1 T539-p RGLDkVItVLtRsKR
0 2 T542-p DkVItVLtRsKRKGS
0 2 S544-p VItVLtRsKRKGSAR
0 1 Y561 PRRLKLHYNVTTTRL
0 1 K632-ub GIRRQRLkGDAWVYk
0 1 K639-m3 kGDAWVYkRLVEDIL
0 2 K650-ub EDILSSCkV______
0 1 K650-m3 EDILSSCkV______
  mouse

 
Y4-p ____MKDyDELLKYY
K44 VAIKIMDKNALGsDL
S49-p MDKNALGsDLPRVKT
K55 GsDLPRVKTEIDALK
T56 sDLPRVKTEIDALKS
K62 KTEIDALKSLRHQHI
K134 GYAHRDLKPENLLFD
K145 LLFDENHKLKLIDFG
Y163 KPKGNKDYHLQTCCG
T167 NKDYHLQTCCGSLAY
S171 HLQTCCGSLAYAAPE
S236 PKWLSPSSILLLQQM
S253 VDPKKRISMRNLLNH
Y267 HPWVMQDYSCPVEWQ
C269 WVMQDYSCPVEWQSK
L335 KPARLQLLSFSCGTA
S336 PARLQLLSFSCGTAS
S338 RLQLLSFSCGTASTT
S343 SFSCGTASTTPKSKN
T345 SCGTASTTPKSKNLs
S348 TASTTPKSKNLsLED
S352-p TPKSKNLsLEDMsts
S357-p NLsLEDMstsDDNCV
T358-p LsLEDMstsDDNCVA
S359-p sLEDMstsDDNCVAG
C363 MstsDDNCVAGLIDy
Y370-p CVAGLIDyELCEDKL
- gap
P383 KLLAPKTPQVTKHLA
K387 PKTPQVTKHLAESNH
A390 PQVTKHLAESNHAAS
S392 VTKHLAESNHAASKs
S397 AESNHAASKsPAPGV
S399-p SNHAASKsPAPGVRR
A401 HAASKsPAPGVRRAV
A407 PAPGVRRAVANKLMD
C419 LMDKENVCTPKSsVK
T420 MDKENVCTPKSsVKN
S423 ENVCTPKSsVKNEEQ
S424-p NVCTPKSsVKNEEQF
K426 CTPKSsVKNEEQFVF
Q430 SsVKNEEQFVFSEPK
I438 FVFSEPKIPVSKNQY
A451 QYKREIPAsPtRFPT
S452-p YKREIPAsPtRFPTP
T454-p REIPAsPtRFPTPAK
T458 AsPtRFPTPAKARAQ
A460 PtRFPTPAKARAQCL
A470 RAQCLREAPVRTPGN
R473 CLREAPVRTPGNSAG
S478 PVRTPGNSAGADTLT
A481 TPGNSAGADTLTTGV
T483 GNSAGADTLTTGVIs
T486 AGADTLTTGVIsPER
S490-p TLTTGVIsPERRCRs
S497-p sPERRCRsMDVDLNQ
T510 NQAHMEDTPKKKGTN
S521-p KGTNVFGsLERGLDK
K528 sLERGLDKVLTALTR
T531 RGLDKVLTALTRNKK
T534 DKVLTALTRNKKKGS
N536 VLTALTRNKKKGSAR
Y553-p PRKRKLHyNVTTTRL
K624 GIRRQRLKGDAWVYK
K631 KGDAWVYKRLVEDIL
K642 EDILSGCKM______
K642 EDILSGCKM______
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