[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1A), AND POSSIBLE FUNCTION.
TISSUE=Brain;
DOI=10.1126/science.277.5326.693; PubMed=9235893 [NCBI, ExPASy, EBI, Israel, Japan]
Dickens M.,
Rogers J.S.,
Cavanagh J.,
Raitano A.,
Xia Z.,
Halpern J.R.,
Greenberg M.E.,
Sawyers C.L.,
Davis R.J.;
"A cytoplasmic inhibitor of the JNK signal transduction pathway.";
Science 277:693-696(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JIP-1B; JIP-1C; JIP-1D AND JIP-1E).
STRAIN=BALB/c;
TISSUE=Brain;
PubMed=10098834 [NCBI, ExPASy, EBI, Israel, Japan]
Kim I.-J.,
Lee K.-W.,
Park B.Y.,
Lee J.-K.,
Park J.,
Choi I.Y.,
Eom S.-J.,
Chang T.-S.,
Kim M.J.,
Yeom Y.I.,
Chang S.K.,
Lee Y.-D.,
Choi E.-J.,
Han P.-L.;
"Molecular cloning of multiple splicing variants of JIP-1 preferentially expressed in brain.";
J. Neurochem. 72:1335-1343(1999).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=10490659 [NCBI, ExPASy, EBI, Israel, Japan]
Yasuda J.,
Whitmarsh A.J.,
Cavanagh J.,
Sharma M.,
Davis R.J.;
"The JIP group of mitogen-activated protein kinase scaffold proteins.";
Mol. Cell. Biol. 19:7245-7254(1999).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND VARIANT ARG-10.
STRAIN=ILS, and ISS;
DOI=10.1007/s00335-001-1001-x; PubMed=11471062 [NCBI, ExPASy, EBI, Israel, Japan]
Ehringer M.A.,
Thompson J.,
Conroy O.,
Xu Y.,
Yang F.,
Canniff J.,
Beeson M.,
Gordon L.,
Bennett B.,
Johnson T.E.,
Sikela J.M.;
"High-throughput sequence identification of gene coding variants within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B).
TISSUE=Brain;
DOI=10.1074/jbc.M108372200; PubMed=11912189 [NCBI, ExPASy, EBI, Israel, Japan]
Taru H.,
Iijima K.,
Hase M.,
Kirino Y.,
Yagi Y.,
Suzuki T.;
"Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade.";
J. Biol. Chem. 277:20070-20078(2002).
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[6]
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INTERACTION WITH RGNEF, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.274.49.35113; PubMed=10574993 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer D.,
Liu A.,
Margolis B.;
"Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons.";
J. Biol. Chem. 274:35113-35118(1999).
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[7]
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TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
DOI=10.1046/j.1460-9568.2000.00945.x; PubMed=10712642 [NCBI, ExPASy, EBI, Israel, Japan]
Pellet J.-B.,
Haefliger J.-A.,
Staple J.K.,
Widmann C.,
Welker E.,
Hirling H.,
Bonny C.,
Nicod P.,
Catsicas S.,
Waeber G.,
Riederer B.M.;
"Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain.";
Eur. J. Neurosci. 12:621-632(2000).
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[8]
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INTERACTION WITH LRPS.
DOI=10.1074/jbc.M000955200; PubMed=10827173 [NCBI, ExPASy, EBI, Israel, Japan]
Gotthardt M.,
Trommsdorff M.,
Nevitt M.F.,
Shelton J.,
Richardson J.A.,
Stockinger W.,
Nimpf J.,
Herz J.;
"Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction.";
J. Biol. Chem. 275:25616-25624(2000).
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[9]
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INTERACTION WITH KLC1.
TISSUE=Brain;
DOI=10.1083/jcb.152.5.959; PubMed=11238452 [NCBI, ExPASy, EBI, Israel, Japan]
Verhey K.J.,
Meyer D.,
Deehan R.,
Blenis J.,
Schnapp B.J.,
Rapoport T.A.,
Margolis B.;
"Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules.";
J. Cell Biol. 152:959-970(2001).
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[10]
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FUNCTION.
DOI=10.1101/gad.922801; PubMed=11562351 [NCBI, ExPASy, EBI, Israel, Japan]
Whitmarsh A.J.,
Kuan C.-Y.,
Kennedy N.J.,
Kelkar N.,
Haydar T.F.,
Mordes J.P.,
Appel M.,
Rossini A.A.,
Jones S.N.,
Flavell R.A.,
Rakic P.,
Davis R.J.;
"Requirement of the JIP1 scaffold protein for stress-induced JNK activation.";
Genes Dev. 15:2421-2432(2001).
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- 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. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interations with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response (By similarity).
- SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely MAPK8, MAPK9, MAPK10, MAP2K7, MAP3K10, MAP3K11 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2) (By similarity). Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Interacts with the cytoplasmic domain of APP (By similarity). Interacts, via the PID domain, with RGNEF.
- INTERACTION:
P05067:APP (xeno); NbExp=1; IntAct=EBI-288461, EBI-77613;
P12023:App; NbExp=2; IntAct=EBI-74515, EBI-78814;
P12023:App; NbExp=2; IntAct=EBI-288461, EBI-78814;
P12023-2:App; NbExp=1; IntAct=EBI-288461, EBI-286828;
P14599:Appl (xeno); NbExp=1; IntAct=EBI-74515, EBI-74135;
P92208:bsk (xeno); NbExp=1; IntAct=EBI-74515, EBI-74487;
Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-74515, EBI-300955;
Q9JLB3:Lrp2; NbExp=1; IntAct=EBI-74515, EBI-300875;
P45983:MAPK8 (xeno); NbExp=1; IntAct=EBI-288461, EBI-286483;
- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, perinuclear region (By similarity). Nucleus (By similarity). Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity).
- ALTERNATIVE PRODUCTS:
5 named isoforms [FASTA] produced by alternative splicing.
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| Name | JIP-1a |
| Synonyms | 1 |
| Isoform ID | Q9WVI9-2 |
| Features which should be applied to build the isoform sequence: VSP_002766. |
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| Name | JIP-1c |
| Synonyms | 2a |
| Isoform ID | Q9WVI9-3 |
| Features which should be applied to build the isoform sequence: VSP_002763. |
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| Name | JIP-1e |
| Synonyms | 3 |
| Isoform ID | Q9WVI9-5 |
| Features which should be applied to build the isoform sequence: VSP_002764. |
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- TISSUE SPECIFICITY: Expressed predominantly in the brain and insulin-secreting cells. In the brain, high expression found in the cerebral cortex and hippocampus. Localizes in the synaptic regions of the olfactory bulb, retina, cerebral and cerebellar cortex and hippocampus. Also expressed in a restricted number of axons, including mossy fibers from the hippocampal dentate gyrus, soma, dendrites and axons of cerebellar Purkinje cells. Also expressed in kidney, testis and prostate. Low levels in heart, ovary and small intestine. Isoform JIP-1b is more predominant in the brain than isoform JIP-1a. Isoform Jip1-a is expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform JIP-1e are brain specific.
- DEVELOPMENTAL STAGE: Low levels at prenatal stage E15, increased levels during the first postnatal days, with a plateau at postnatal day 15.
- INDUCTION: Upon neuron differentiation.
- PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12.
- PTM: Ubiquitinated. Two preliminary events are required to prime for ubiquitination; phosphorylation and an increased in intracellular calcium concentration. Then, the calcium influx initiates ubiquitination and degradation by the ubiquitin-proteasome pathway.
- SIMILARITY: Belongs to the JIP scaffold family.
- SIMILARITY: Contains 1 PID domain.
- SIMILARITY: Contains 1 SH3 domain.
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