Protein detail
MARK2
Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)
Protein symbol MARK2 | UniProt ID | EVMP score 0.50 |
Frequency 5 | Transmembrane count | Protein classification EnzymesPredicted intracellular proteins |
Basic Information
Protein Names
Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)
Protein Class
EnzymesPredicted intracellular proteins
Protein Function
- ENZYME proteins:Transferases
- Enzymes
- Predicted intracellular proteins
- Kinases:CAMK Ser/Thr protein kinases
Ensembl
Entrez Gene Symbol
Gene Synonym
EMK1PAR-1PAR-1BPar1b
Gene Description
Microtubule affinity regulating kinase 2
Chromosome
11
Position
63838928-63911020
Frequency
5
EVMP Score
0.50
Fluorescence & Localization
Tissue Specificblood vesselCell SpecificAlveolar cells type 1Single-Nuclei Brain Specificendothelial cell
Function & Pathway
Protein Function
- ENZYME proteins:Transferases
- Enzymes
- Predicted intracellular proteins
- Kinases:CAMK Ser/Thr protein kinases
Cellular Component
Molecular Function
- GO:0000287 magnesium ion binding
- GO:0003723 RNA binding
- GO:0004674 protein serine/threonine kinase activity
- GO:0005515 protein binding
- GO:0005524 ATP binding
- GO:0008289 lipid binding
- GO:0030295 protein kinase activator activity
- GO:0044024 histone H2AS1 kinase activity
- GO:0045296 cadherin binding
- GO:0048156 tau protein binding
- GO:0050321 tau-protein kinase activity
- GO:0106310 protein serine kinase activity
Biological Process
Mediation Categories
Receptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
20 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| MARK2 | STK11 | Q15831 | T | 208 | phosphorylation | BEL-Large-Corpus_ProtMapperPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperdbPTMKEAphosphoELMSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | dbPTM:17192257phosphoELM:14976552dbPTM:19369195ProtMapper:14976552dbPTM:14976552KEA:17192257KEA:14976552SIGNOR:14976552 |
| MARK2 | STK11 | Q15831 | T | 175 | phosphorylation | KEA | KEA:14976552 |
| MARK2 | PRKCA | P17252 | T | 596 | phosphorylation | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPKEAphosphoELM | KEA:15324659phosphoELM:15324659 |
| MARK2 | PRKCA | P17252 | S | 409 | phosphorylation | PhosphoNetworks | |
| MARK2 | PRKCA | P17252 | T | 603 | phosphorylation | PhosphoNetworks | |
| MARK2 | PRKCA | P17252 | T | 508 | phosphorylation | KEA | KEA:15324659 |
| MARK2 | PRKCA | P17252 | T | 562 | phosphorylation | KEA | KEA:15324659 |
| MARK2 | PRKCA | P17252 | T | 563 | phosphorylation | KEA | KEA:15324659 |
| MARK2 | TAOK1 | Q7L7X3 | T | 208 | phosphorylation | dbPTM | dbPTM:17192257dbPTM:14976552dbPTM:19369195 |
| MARK2 | PRKCZ | Q05513 | T | 596 | phosphorylation | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | KEA:15324659SIGNOR:15084291ProtMapper:15084291 |
Page 1 of 2Next
Ligand-Receptor Signaling
12 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor | receptor | OmniPath | No | Yes | No | No | No |
| intracellular | intracellular | LOCATE | No | No | No | No | No |
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | LOCATE | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
| lateral_cell_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
Page 1 of 2Next
Regulatory Interaction Network
24 records.
Protein Complex Composition
13 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| EXO1HSPA4MARK1MARK2MARK3MARK4PRKAA1STK11WDR89YWHABYWHAEYWHAGYWHAHYWHAQYWHAZ | P27348P27448P31946P34932P61981P62258P63104Q04917Q13131Q15831Q7KZI7Q96FK6Q96L34Q9P0L2Q9UQ84 | 1:1:1:1:1:1:1:1:1:1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC9070 | ||
| MARK2 | Q7KZI7 | 2 | PDB | PDB:5kz8PDB:5kz7PDB:8txyPDB:5eak | ||
| CDK15MARK2 | Q7KZI7Q96Q40 | 0:0 | hu.MAP |
Page 2 of 2Previous
Isolation & Detection Technology
Sequence, Structure & Domains
Sequences
Length
788
Mass
87,911
Sequence
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
Alternative Products
Event=Alternative promoter usage, Alternative splicing; Named isoforms=16; Name=1; Synonyms=Alpha; IsoId=Q7KZI7-1; Sequence=Displayed; Name=2; IsoId=Q7KZI7-2; Sequence=VSP_051705, VSP_051706; Name=3; IsoId=Q7KZI7-3; Sequence=VSP_051705, VSP_051707; Name=4; Synonyms=Par-1Balpha; IsoId=Q7KZI7-4; Sequence=VSP_051706, VSP_051707; Name=5; IsoId=Q7KZI7-5; Sequence=VSP_051706, VSP_051708; Name=6; Synonyms=Beta; IsoId=Q7KZI7-6; Sequence=VSP_051705; Name=7; IsoId=Q7KZI7-7; Sequence=VSP_051705, VSP_051706, VSP_051707; Name=8; IsoId=Q7KZI7-8; Sequence=VSP_051707; Name=9; IsoId=Q7KZI7-9; Sequence=VSP_051706; Name=10; IsoId=Q7KZI7-10; Sequence=VSP_051705, VSP_051706, VSP_051708; Name=11; IsoId=Q7KZI7-11; Sequence=VSP_051708; Name=12; IsoId=Q7KZI7-12; Sequence=VSP_051705, VSP_051708; Name=13; IsoId=Q7KZI7-13; Sequence=VSP_051705, VSP_039872, VSP_051706, VSP_051707; Name=14; IsoId=Q7KZI7-14; Sequence=VSP_051705, VSP_039872, VSP_051707; Name=15; IsoId=Q7KZI7-15; Sequence=VSP_039872, VSP_051706, VSP_041853; Name=16; IsoId=Q7KZI7-16; Sequence=VSP_039872, VSP_051706, VSP_051707
Alternative Sequence
1..33; Missing (in isoform 2, isoform 3, isoform 6, isoform 7, isoform 10, isoform 12, isoform 13 and isoform 14); 412; Missing (in isoform 13, isoform 14, isoform 15 and isoform 16); 505..558; Missing (in isoform 2, isoform 4, isoform 5, isoform 7, isoform 9, isoform 10, isoform 13, isoform 15 and isoform 16); 644..652; Missing (in isoform 3, isoform 4, isoform 7, isoform 8, isoform 13, isoform 14 and isoform 16); 645..668; Missing (in isoform 15); 654..668; Missing (in isoform 5, isoform 11, isoform 10 and isoform 12)
3D Structural Models
Turn
73..75
Helix
86..88; 93..106; 137..144; 149..168; 178..180; 213..215; 218..222; 230..245; 255..264; 275..284; 289..291; 295..298; 303..305; 326..335; 339..347; 353..360
Beta Strand
53..60; 63..72; 78..85; 115..120; 122..130; 181..183; 189..191; 309..311
3D Structure
X-ray crystallography (5)
Domain & Motif Annotations
Compositional Bias
27..45; Polar residues; 418..432; Polar residues; 433..445; Basic and acidic residues; 467..486; Polar residues; 495..504; Polar residues; 511..525; Low complexity
Domain (CC)
The UBA domain does not seem to bind ubiquitin and ubiquitin-like and might play a role in regulating the enzyme conformation and localization. Activation of the kinase activity following phosphorylation at Thr-208 is accompanied by a conformational change that alters the orientation of the UBA domain with respect to the catalytic domain.; DOMAIN: The KA1 domain mediates binding to phospholipids and targeting to membranes.
Domain (FT)
53..304; Protein kinase; 323..362; UBA; 739..788; KA1
Region
1..46; Disordered; 373..632; Disordered
Protein Families
- Protein kinase superfamily
- CAMK Ser/Thr protein kinase family
- SNF1 subfamily
Sequence Similarities
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
Clinical Relevance
Drugs
Interaction Protein
ENSG00000108953ENSG00000128245ENSG00000134308ENSG00000152818ENSG00000164924ENSG00000166913ENSG00000168502ENSG00000170027
Interaction Count
8
Interaction Dataset
biogrid_opencellintact_biogrid_opencellintact_biogrid