Q99JP0 · M4K3_MOUSE
- ProteinMitogen-activated protein kinase kinase kinase kinase 3
- GeneMap4k3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids894 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Serine/threonine kinase that plays a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | MAP kinase kinase kinase kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | SH3 domain binding | |
Biological Process | intracellular signal transduction | |
Biological Process | protein phosphorylation | |
Biological Process | response to UV |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase kinase kinase kinase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99JP0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000086278 | 1-894 | Mitogen-activated protein kinase kinase kinase kinase 3 | |||
Sequence: MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKLKWSNSFHHFVKMALTKNPKKRPNAEKLLQHPFVTQPLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIPSTSRNVREEKTRSEINFGQVKFDPPLRKETEPHHELPDSDGFFDSSEEIYYTARSNLDLQLEYGQGHQSHCFLGGNKSLLKSVEEELHQRGHVAHLEDDEGDDDDSKHSTMKAKVPPPLPPKPKSIFIPQDTHSAEDGNQGTIKRCPSSGSPAKPSHVPPRPPPPRLPPQKPAVLGNGVNSFQLNGERDGSLYQQQSEQRGTNLSRKEKKDVPKPISNGLPPTPKVHMGACFSKVFNGCPLKIHCATSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSVSGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFAVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIEFPMPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDAPQTSVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDNTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY | ||||||
Modified residue | 329 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 398 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with SH3GL2. Interaction appears to regulate MAP4K3-mediated JNK activation (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q99JP0 | LCP2 Q13094 | 2 | EBI-5324222, EBI-346946 | |
BINARY | Q99JP0 | Prkcq Q02111 | 2 | EBI-5324222, EBI-2639157 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-273 | Protein kinase | ||||
Sequence: FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKLKWSNSFHHFVKMALTKNPKKRPNAEKLLQHPFV | ||||||
Region | 339-358 | Disordered | ||||
Sequence: DPPLRKETEPHHELPDSDGF | ||||||
Compositional bias | 340-357 | Basic and acidic residues | ||||
Sequence: PPLRKETEPHHELPDSDG | ||||||
Compositional bias | 408-427 | Basic and acidic residues | ||||
Sequence: HVAHLEDDEGDDDDSKHSTM | ||||||
Region | 408-537 | Disordered | ||||
Sequence: HVAHLEDDEGDDDDSKHSTMKAKVPPPLPPKPKSIFIPQDTHSAEDGNQGTIKRCPSSGSPAKPSHVPPRPPPPRLPPQKPAVLGNGVNSFQLNGERDGSLYQQQSEQRGTNLSRKEKKDVPKPISNGLP | ||||||
Compositional bias | 448-465 | Polar residues | ||||
Sequence: THSAEDGNQGTIKRCPSS | ||||||
Compositional bias | 469-487 | Pro residues | ||||
Sequence: AKPSHVPPRPPPPRLPPQK | ||||||
Compositional bias | 492-517 | Polar residues | ||||
Sequence: GNGVNSFQLNGERDGSLYQQQSEQRG | ||||||
Domain | 556-867 | CNH | ||||
Sequence: PLKIHCATSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSVSGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFAVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIEFPMPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDAPQTSVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDNTRIFRLLGSDRV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length894
- Mass (Da)101,119
- Last updated2011-07-27 v4
- ChecksumA9D9086ADC9DDA4F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q4EGQ9 | A0A3Q4EGQ9_MOUSE | Map4k3 | 873 | ||
E9QNE9 | E9QNE9_MOUSE | Map4k3 | 896 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 340-357 | Basic and acidic residues | ||||
Sequence: PPLRKETEPHHELPDSDG | ||||||
Compositional bias | 408-427 | Basic and acidic residues | ||||
Sequence: HVAHLEDDEGDDDDSKHSTM | ||||||
Compositional bias | 448-465 | Polar residues | ||||
Sequence: THSAEDGNQGTIKRCPSS | ||||||
Compositional bias | 469-487 | Pro residues | ||||
Sequence: AKPSHVPPRPPPPRLPPQK | ||||||
Compositional bias | 492-517 | Polar residues | ||||
Sequence: GNGVNSFQLNGERDGSLYQQQSEQRG | ||||||
Sequence conflict | 874 | in Ref. 3; AAH05781 | ||||
Sequence: P → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC131712 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC169501 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK014711 EMBL· GenBank· DDBJ | BAB29516.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005781 EMBL· GenBank· DDBJ | AAH05781.1 EMBL· GenBank· DDBJ | mRNA |