Q9ERE9 · JIP2_MOUSE
- ProteinC-Jun-amino-terminal kinase-interacting protein 2
- GeneMapk8ip2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids830 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Names & Taxonomy
Protein names
- Recommended nameC-Jun-amino-terminal kinase-interacting protein 2
- Short namesJIP-2; JNK-interacting protein 2
- 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 accessionQ9ERE9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Accumulates in cell surface projections.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000220632 | 1-830 | C-Jun-amino-terminal kinase-interacting protein 2 | |||
Sequence: MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEEEEEEEEEEEDGDRQGKAGGGPGSQALAGDSLIPSPSLEESHKLRPTTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLRSPAQEPLKELPAPLLPAEEERHEVQSLARPGCDCEGNQPPEPPASSGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSGRSSHLTNSIEEASSPASEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRLPEEAASQANSVPQDCQDPEAGPHVELVDMDTLCGPPPPAPAAPRLGPAQPGPCLFLSNPTRDTITPLWATPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVVPPGSRTTGSTAPLDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLGNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCVVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLAFACPTEDIYLE | ||||||
Modified residue | 257 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 304 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 307 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in brain. Expressed in all neurons. Also expressed in testis, primarily in the epididymal epidermis.
Induction
Upon neuron differentiation.
Gene expression databases
Interaction
Subunit
Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely JNK1, JNK2, JNK3, MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13 (By similarity).
Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Interacts with DCLK2. Interacts with FGF13; enables the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding activity. Interacts with TIAM1 and TIAM2 (PubMed:10827199, PubMed:11378392, PubMed:16628014, PubMed:19893486).
Interacts with SH3RF2 (By similarity).
Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Interacts with DCLK2. Interacts with FGF13; enables the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding activity. Interacts with TIAM1 and TIAM2 (PubMed:10827199, PubMed:11378392, PubMed:16628014, PubMed:19893486).
Interacts with SH3RF2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9ERE9 | Appl P14599 | 2 | EBI-74576, EBI-74135 | |
BINARY | Q9ERE9 | Lrp1 Q91ZX7 | 2 | EBI-74576, EBI-300955 | |
BINARY | Q9ERE9 | Lrp2 A2ARV4 | 2 | EBI-74576, EBI-300875 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MADRAEMFSLSTFHSLSPPGCRPPQD | ||||||
Region | 44-354 | Disordered | ||||
Sequence: CGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEEEEEEEEEEEDGDRQGKAGGGPGSQALAGDSLIPSPSLEESHKLRPTTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLRSPAQEPLKELPAPLLPAEEERHEVQSLARPGCDCEGNQPPEPPASSGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSGRSSHLTNSIEEASSPASEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSP | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: SYDSDHCEKDSLSLG | ||||||
Compositional bias | 79-105 | Acidic residues | ||||
Sequence: QEFEMIDDNEEEDDEEEEEEEEEEEDG | ||||||
Region | 111-278 | JNK-binding domain (JBD) | ||||
Sequence: AGGGPGSQALAGDSLIPSPSLEESHKLRPTTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLRSPAQEPLKELPAPLLPAEEERHEVQSLARPGCDCEGNQPPEPPASSGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETE | ||||||
Compositional bias | 140-174 | Polar residues | ||||
Sequence: TTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLR | ||||||
Compositional bias | 188-202 | Basic and acidic residues | ||||
Sequence: LLPAEEERHEVQSLA | ||||||
Region | 242-504 | Necessary for interaction with FGF13 | ||||
Sequence: GHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSGRSSHLTNSIEEASSPASEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRLPEEAASQANSVPQDCQDPEAGPHVELVDMDTLCGPPPPAPAAPRLGPAQPGPCLFLSNPTRDTITPLWATPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVVPPGSRTTGSTA | ||||||
Compositional bias | 275-304 | Polar residues | ||||
Sequence: SETELELSSDGGSSSGRSSHLTNSIEEASS | ||||||
Region | 367-438 | Disordered | ||||
Sequence: EGSSPIRCPGQCLSPAPRLPEEAASQANSVPQDCQDPEAGPHVELVDMDTLCGPPPPAPAAPRLGPAQPGPC | ||||||
Compositional bias | 418-432 | Pro residues | ||||
Sequence: CGPPPPAPAAPRLGP | ||||||
Region | 452-504 | Disordered | ||||
Sequence: LWATPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVVPPGSRTTGSTA | ||||||
Compositional bias | 471-490 | Acidic residues | ||||
Sequence: SEEEEEDEEEDEEDEEDAED | ||||||
Region | 539-574 | Disordered | ||||
Sequence: GNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSP | ||||||
Domain | 610-671 | SH3 | ||||
Sequence: EREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPG | ||||||
Domain | 683-819 | PID | ||||
Sequence: PCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLA |
Sequence similarities
Belongs to the JIP scaffold family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length830
- Mass (Da)89,900
- Last updated2001-03-01 v1
- Checksum7EC8EAD19A90163C
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: SYDSDHCEKDSLSLG | ||||||
Compositional bias | 79-105 | Acidic residues | ||||
Sequence: QEFEMIDDNEEEDDEEEEEEEEEEEDG | ||||||
Compositional bias | 140-174 | Polar residues | ||||
Sequence: TTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLR | ||||||
Compositional bias | 188-202 | Basic and acidic residues | ||||
Sequence: LLPAEEERHEVQSLA | ||||||
Sequence conflict | 216 | in Ref. 2; AK014339 | ||||
Sequence: P → Q | ||||||
Compositional bias | 275-304 | Polar residues | ||||
Sequence: SETELELSSDGGSSSGRSSHLTNSIEEASS | ||||||
Compositional bias | 418-432 | Pro residues | ||||
Sequence: CGPPPPAPAAPRLGP | ||||||
Compositional bias | 471-490 | Acidic residues | ||||
Sequence: SEEEEEDEEEDEEDEEDAED |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF310135 EMBL· GenBank· DDBJ | AAG31800.1 EMBL· GenBank· DDBJ | mRNA | ||
AK014339 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |