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Entry version 185 (18 Sep 2019)
Sequence version 3 (19 Jul 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei40ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei132Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi17 – 25ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle
LigandATP-binding, Calcium, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q14680

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q14680

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MELK
Synonyms:KIAA0175
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:16870 MELK

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
607025 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q14680

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
9833

Open Targets

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OpenTargetsi
ENSG00000165304

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134902874

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4578

Drug and drug target database

More...
DrugBanki
DB12010 Fostamatinib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2102

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MELK

Domain mapping of disease mutations (DMDM)

More...
DMDMi
50400857

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000863231 – 651Maternal embryonic leucine zipper kinaseAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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 autocatalysisCombined sources2 Publications1
Modified residuei539Phosphothreonine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

The CPTAC Assay portal

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CPTACi
CPTAC-1169

Encyclopedia of Proteome Dynamics

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EPDi
Q14680

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q14680

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q14680

MaxQB - The MaxQuant DataBase

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MaxQBi
Q14680

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q14680

PeptideAtlas

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PeptideAtlasi
Q14680

PRoteomics IDEntifications database

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PRIDEi
Q14680

ProteomicsDB human proteome resource

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ProteomicsDBi
1664
1665
25479
26046
27114
60115 [Q14680-1]
6817
6894

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q14680

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q14680

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in placenta, kidney, thymus, testis, ovary and intestine.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Increases during G2/M phase compared to interphase. Protein level decreases when cells exit mitosis, probably due to degradation.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000165304 Expressed in 142 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q14680 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q14680 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA017214

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Interacts with ZNF622 and PPP1R8.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2L14Q9BZR84EBI-1046702,EBI-1385773

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115171, 60 interactors

Protein interaction database and analysis system

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IntActi
Q14680, 17 interactors

Molecular INTeraction database

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MINTi
Q14680

STRING: functional protein association networks

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STRINGi
9606.ENSP00000298048

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q14680

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q14680

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini11 – 263Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini602 – 651KA1PROSITE-ProRule annotationAdd BLAST50

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni282 – 321UBA-likeAdd BLAST40
Regioni326 – 651Autoinhibitory regionAdd BLAST326

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The KA1 domain mediates binding to phospholipids and targeting to membranes.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0583 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154889

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233023

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q14680

KEGG Orthology (KO)

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KOi
K08799

Identification of Orthologs from Complete Genome Data

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OMAi
ELMTCCG

Database of Orthologous Groups

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OrthoDBi
1127668at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q14680

TreeFam database of animal gene trees

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TreeFami
TF314032

Family and domain databases

Conserved Domains Database

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CDDi
cd14078 STKc_MELK, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR028375 KA1/Ssp2_C
IPR001772 KA1_dom
IPR011009 Kinase-like_dom_sf
IPR034673 MELK
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF02149 KA1, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF103243 SSF103243, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50032 KA1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 8 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q14680-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0D9SFF9A0A0D9SFF9_HUMAN
Maternal embryonic leucine zipper k...
MELK
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0D9SFL8A0A0D9SFL8_HUMAN
Maternal embryonic leucine zipper k...
MELK
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0D9SGI4A0A0D9SGI4_HUMAN
Maternal embryonic leucine zipper k...
MELK
215Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0D9SFB9A0A0D9SFB9_HUMAN
Maternal embryonic leucine zipper k...
MELK
165Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA11492 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04079456T → M1 PublicationCorresponds to variant dbSNP:rs35233455Ensembl.1
Natural variantiVAR_040795219K → R1 PublicationCorresponds to variant dbSNP:rs35142210Ensembl.1
Natural variantiVAR_040796333R → K1 PublicationCorresponds to variant dbSNP:rs34655121Ensembl.1
Natural variantiVAR_040797348T → I1 PublicationCorresponds to variant dbSNP:rs55845414Ensembl.1
Natural variantiVAR_040798460T → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs144052967Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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 Genomic DNA No translation available.
AL442063 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58303.1
CH471071 Genomic DNA Translation: EAW58304.1
BC014039 mRNA Translation: AAH14039.1

The Consensus CDS (CCDS) project

More...
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]
CCDS6606.1 [Q14680-1]

NCBI Reference Sequences

More...
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]
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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000298048; 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]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9833

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9833

UCSC genome browser

More...
UCSCi
uc003zzn.5 human [Q14680-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 Genomic DNA No translation available.
AL442063 Genomic DNA No translation available.
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5K00X-ray1.77A3-330[»]
5M5AX-ray1.90A2-340[»]
5MAFX-ray2.80A2-340[»]
5MAGX-ray2.35A2-340[»]
5MAHX-ray2.00A2-340[»]
5MAIX-ray2.15A2-340[»]
5TVTX-ray2.28A2-333[»]
5TWLX-ray2.42A2-340[»]
5TWUX-ray2.60A/B1-340[»]
5TWYX-ray2.91A/B2-340[»]
5TWZX-ray2.63A2-340[»]
5TX3X-ray2.90A/B1-340[»]
6GVXX-ray2.24A/B1-340[»]
SMRiQ14680
ModBaseiSearch...

Protein-protein interaction databases

BioGridi115171, 60 interactors
IntActiQ14680, 17 interactors
MINTiQ14680
STRINGi9606.ENSP00000298048

Chemistry databases

BindingDBiQ14680
ChEMBLiCHEMBL4578
DrugBankiDB12010 Fostamatinib

DrugCentral

More...
DrugCentrali
Q14680
GuidetoPHARMACOLOGYi2102

PTM databases

iPTMnetiQ14680
PhosphoSitePlusiQ14680

Polymorphism and mutation databases

BioMutaiMELK
DMDMi50400857

Proteomic databases

CPTACiCPTAC-1169
EPDiQ14680
jPOSTiQ14680
MassIVEiQ14680
MaxQBiQ14680
PaxDbiQ14680
PeptideAtlasiQ14680
PRIDEiQ14680
ProteomicsDBi1664
1665
25479
26046
27114
60115 [Q14680-1]
6817
6894

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
9833
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

Comparative Toxicogenomics Database

More...
CTDi
9833
DisGeNETi9833

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MELK
HGNCiHGNC:16870 MELK
HPAiHPA017214
MIMi607025 gene
neXtProtiNX_Q14680
OpenTargetsiENSG00000165304
PharmGKBiPA134902874

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000154889
HOGENOMiHOG000233023
InParanoidiQ14680
KOiK08799
OMAiELMTCCG
OrthoDBi1127668at2759
PhylomeDBiQ14680
TreeFamiTF314032

Enzyme and pathway databases

SignaLinkiQ14680
SIGNORiQ14680

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MELK human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MELK

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
9833

Pharos

More...
Pharosi
Q14680

Protein Ontology

More...
PROi
PR:Q14680

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165304 Expressed in 142 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ14680 baseline and differential
GenevisibleiQ14680 HS

Family and domain databases

CDDicd14078 STKc_MELK, 1 hit
InterProiView protein in InterPro
IPR028375 KA1/Ssp2_C
IPR001772 KA1_dom
IPR011009 Kinase-like_dom_sf
IPR034673 MELK
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF02149 KA1, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF103243 SSF103243, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50032 KA1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMELK_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q14680
Secondary accession number(s): A6P3A7
, A6P3A8, B1AMQ6, B7Z1E6, B7Z5M5, B7Z6Q7, B7Z6R8, B7Z6Y0, B7Z7Q1, D3DRP8, F5H0Y0, F5H2R4, F5H689, Q7L3C3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: September 18, 2019
This is version 185 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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