Q9ERE9 · JIP2_MOUSE

  • Protein
    C-Jun-amino-terminal kinase-interacting protein 2
  • Gene
    Mapk8ip2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentneuronal cell body
Cellular Componentpostsynaptic density
Cellular Componentprotein-containing complex
Molecular FunctionJUN kinase binding
Molecular Functionkinesin binding
Molecular FunctionMAP-kinase scaffold activity
Molecular Functionprotein kinase activator activity
Molecular Functionprotein kinase binding
Molecular Functionprotein-containing complex binding
Biological Processbehavioral fear response
Biological Processdendrite morphogenesis
Biological Processexcitatory postsynaptic potential
Biological ProcessJNK cascade
Biological ProcessMAPK cascade
Biological Processmating behavior
Biological Processnegative regulation of apoptotic signaling pathway
Biological Processnonassociative learning
Biological Processpositive regulation of stress-activated MAPK cascade
Biological Processregulation of AMPA receptor activity
Biological Processregulation of JNK cascade
Biological Processregulation of NMDA receptor activity
Biological Processregulation of signaling receptor activity
Biological Processregulation of synaptic transmission, glutamatergic
Biological Processsocial behavior

Names & Taxonomy

Protein names

  • Recommended name
    C-Jun-amino-terminal kinase-interacting protein 2
  • Short names
    JIP-2; JNK-interacting protein 2
  • Alternative names
    • Islet-brain-2 (IB-2)
    • JNK MAP kinase scaffold protein 2
    • Mitogen-activated protein kinase 8-interacting protein 2

Gene names

    • Name
      Mapk8ip2
    • Synonyms
      Ib2, Jip2

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9ERE9
  • Secondary accessions
    • Q9CXI4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002206321-830C-Jun-amino-terminal kinase-interacting protein 2
Modified residue257Phosphoserine
Modified residue304Phosphoserine
Modified residue307Phosphoserine

Keywords

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q9ERE9Appl P145992EBI-74576, EBI-74135
BINARY Q9ERE9Lrp1 Q91ZX72EBI-74576, EBI-300955
BINARY Q9ERE9Lrp2 A2ARV42EBI-74576, EBI-300875

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-26Disordered
Region44-354Disordered
Compositional bias49-63Basic and acidic residues
Compositional bias79-105Acidic residues
Region111-278JNK-binding domain (JBD)
Compositional bias140-174Polar residues
Compositional bias188-202Basic and acidic residues
Region242-504Necessary for interaction with FGF13
Compositional bias275-304Polar residues
Region367-438Disordered
Compositional bias418-432Pro residues
Region452-504Disordered
Compositional bias471-490Acidic residues
Region539-574Disordered
Domain610-671SH3
Domain683-819PID

Sequence similarities

Belongs to the JIP scaffold family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    830
  • Mass (Da)
    89,900
  • Last updated
    2001-03-01 v1
  • Checksum
    7EC8EAD19A90163C
MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEEEEEEEEEEEDGDRQGKAGGGPGSQALAGDSLIPSPSLEESHKLRPTTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLRSPAQEPLKELPAPLLPAEEERHEVQSLARPGCDCEGNQPPEPPASSGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSGRSSHLTNSIEEASSPASEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRLPEEAASQANSVPQDCQDPEAGPHVELVDMDTLCGPPPPAPAAPRLGPAQPGPCLFLSNPTRDTITPLWATPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVVPPGSRTTGSTAPLDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLGNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCVVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLAFACPTEDIYLE

Sequence caution

The sequence AK014339 differs from that shown. Reason: Erroneous termination Truncated C-terminus.

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias49-63Basic and acidic residues
Compositional bias79-105Acidic residues
Compositional bias140-174Polar residues
Compositional bias188-202Basic and acidic residues
Sequence conflict216in Ref. 2; AK014339
Compositional bias275-304Polar residues
Compositional bias418-432Pro residues
Compositional bias471-490Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF310135
EMBL· GenBank· DDBJ
AAG31800.1
EMBL· GenBank· DDBJ
mRNA
AK014339
EMBL· GenBank· DDBJ
-mRNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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