Q03141 · MARK3_MOUSE
- ProteinMAP/microtubule affinity-regulating kinase 3
- GeneMark3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids753 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase. Involved in the specific phosphorylation of microtubule-associated proteins for MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU. Phosphorylates CDC25C on 'Ser-216'. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Regulates localization and activity of MITF by mediating its phosphorylation, promoting subsequent interaction between MITF and 14-3-3 and retention in the cytosol. Negatively regulates the Hippo signaling pathway and antagonizes the phosphorylation of LATS1. Cooperates with DLG5 to inhibit the kinase activity of STK3/MST2 toward LATS1. Phosphorylates PKP2 and KSR1.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by phosphorylation on Thr-211. Inhibited by phosphorylation on Thr-564 (By similarity).
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | dendrite | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | tau-protein kinase activity | |
Biological Process | intracellular signal transduction | |
Biological Process | negative regulation of hippo signaling | |
Biological Process | negative regulation of protein localization to nucleus | |
Biological Process | peptidyl-serine autophosphorylation | |
Biological Process | peptidyl-serine phosphorylation | |
Biological Process | positive regulation of protein binding | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMAP/microtubule affinity-regulating kinase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ03141
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086305 | 1-753 | MAP/microtubule affinity-regulating kinase 3 | |||
Sequence: MSTRTPLPTVNERDTENHISHGDGRQEVTSRTGRSGARCRNSIASCADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPVKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSAELDASDSSSSSNLSLAKVRPNSDLSNSTGQSPHHKGQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGIPSRKSSSSAVGGKGIAPASPMLGNAGNPNKADIPERKKSPAVPSSNTASGGMTRRNTYVCSERCAADRHSVIQNGKENSAIPDERTPVASTHSISSATTPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRNMSFRFIKRLPTEYERNGRYEGSSRNVSSEQKDENREAKPRSLRFTWSMKTTSSMDPSDMMREIRKVLDANNCDYEQRERFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL | ||||||
Modified residue | 42 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 211 | Phosphothreonine; by LKB1 | ||||
Sequence: T | ||||||
Modified residue | 368 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 374 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 380 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 383 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 400 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 419 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 469 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 540 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 543 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 549 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 564 | Phosphothreonine; by PKC/PRKCZ | ||||
Sequence: T | ||||||
Modified residue | 583 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 598 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 601 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 643 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-564 by PRKCZ/aPKC inhibits the kinase activity (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with MAPT/TAU (By similarity).
Interacts with DLG5 (via coiled-coil domain) (By similarity).
Interacts with STK3/MST2 and STK4/MST1 in the presence of DLG5 (By similarity).
Interacts with YWHAB, YWHAG, YWHAQ and YWHAZ (By similarity).
Interacts with PKP2 (via N-terminus) (By similarity).
Interacts with CDC25C (By similarity).
Interacts with KSR1 (PubMed:12941695).
Interacts with DLG5 (via coiled-coil domain) (By similarity).
Interacts with STK3/MST2 and STK4/MST1 in the presence of DLG5 (By similarity).
Interacts with YWHAB, YWHAG, YWHAQ and YWHAZ (By similarity).
Interacts with PKP2 (via N-terminus) (By similarity).
Interacts with CDC25C (By similarity).
Interacts with KSR1 (PubMed:12941695).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Disordered | ||||
Sequence: MSTRTPLPTVNERDTENHISHGDGRQEVTSRTGRS | ||||||
Compositional bias | 14-28 | Basic and acidic residues | ||||
Sequence: DTENHISHGDGRQEV | ||||||
Domain | 56-307 | Protein kinase | ||||
Sequence: YRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPVKRGTLEQIMKDRWI | ||||||
Domain | 326-365 | UBA | ||||
Sequence: ISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLG | ||||||
Compositional bias | 372-418 | Polar residues | ||||
Sequence: DASDSSSSSNLSLAKVRPNSDLSNSTGQSPHHKGQRSVSSSQKQRRY | ||||||
Region | 372-504 | Disordered | ||||
Sequence: DASDSSSSSNLSLAKVRPNSDLSNSTGQSPHHKGQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGIPSRKSSSSAVGGKGIAPASPMLGNAGNPNKADIPERKKSPAVPSSNTASGGMTR | ||||||
Compositional bias | 490-504 | Polar residues | ||||
Sequence: PAVPSSNTASGGMTR | ||||||
Region | 521-604 | Disordered | ||||
Sequence: VIQNGKENSAIPDERTPVASTHSISSATTPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNL | ||||||
Compositional bias | 522-552 | Polar residues | ||||
Sequence: IQNGKENSAIPDERTPVASTHSISSATTPDR | ||||||
Compositional bias | 578-604 | Polar residues | ||||
Sequence: NGPPASPSLSHEATPLSQTRSRGSTNL | ||||||
Region | 632-656 | Disordered | ||||
Sequence: NGRYEGSSRNVSSEQKDENREAKPR | ||||||
Domain | 695-744 | KA1 | ||||
Sequence: RFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIA |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q03141-1
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.
- Name1
- Length753
- Mass (Da)84,390
- Last updated2005-11-08 v2
- ChecksumB597BDD0398617CF
Q03141-2
- Name2
- SynonymsELKL motif kinase 2 short form
- Differences from canonical
- 615-638: Missing
Q03141-3
- Name3
- SynonymsELKL motif kinase 2 long form
- Differences from canonical
- 615-623: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1Y7VNZ6 | A0A1Y7VNZ6_MOUSE | Mark3 | 797 | ||
A0A1Y7VK86 | A0A1Y7VK86_MOUSE | Mark3 | 54 | ||
A0A1Y7VJB1 | A0A1Y7VJB1_MOUSE | Mark3 | 111 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 14-28 | Basic and acidic residues | ||||
Sequence: DTENHISHGDGRQEV | ||||||
Sequence conflict | 333 | in Ref. 2; BAC35922 | ||||
Sequence: D → V | ||||||
Compositional bias | 372-418 | Polar residues | ||||
Sequence: DASDSSSSSNLSLAKVRPNSDLSNSTGQSPHHKGQRSVSSSQKQRRY | ||||||
Compositional bias | 490-504 | Polar residues | ||||
Sequence: PAVPSSNTASGGMTR | ||||||
Sequence conflict | 496 | in Ref. 1; AAF64456 | ||||
Sequence: N → S | ||||||
Sequence conflict | 511 | in Ref. 2; BAC35922 | ||||
Sequence: S → G | ||||||
Compositional bias | 522-552 | Polar residues | ||||
Sequence: IQNGKENSAIPDERTPVASTHSISSATTPDR | ||||||
Compositional bias | 578-604 | Polar residues | ||||
Sequence: NGPPASPSLSHEATPLSQTRSRGSTNL | ||||||
Alternative sequence | VSP_016141 | 615-623 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_016140 | 615-638 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 684 | in Ref. 2; BAC35922 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF240783 EMBL· GenBank· DDBJ | AAF64456.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075742 EMBL· GenBank· DDBJ | BAC35922.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK132247 EMBL· GenBank· DDBJ | BAE21056.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166157 EMBL· GenBank· DDBJ | BAE38602.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026445 EMBL· GenBank· DDBJ | AAH26445.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
X57244 EMBL· GenBank· DDBJ | CAA40520.1 EMBL· GenBank· DDBJ | mRNA |