JIP1_MOUSE
ID JIP1_MOUSE Reviewed; 707 AA.
AC Q9WVI9; O35145; Q925J8; Q9R1H9; Q9R1Z1; Q9WVI7; Q9WVI8;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 1;
DE Short=JIP-1;
DE Short=JNK-interacting protein 1;
DE AltName: Full=Islet-brain-1;
DE Short=IB-1;
DE AltName: Full=JNK MAP kinase scaffold protein 1;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 1;
GN Name=Mapk8ip1; Synonyms=Ib1, Jip1, Mapk8ip, Prkm8ip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1A), AND POSSIBLE FUNCTION.
RC TISSUE=Brain;
RX PubMed=9235893; DOI=10.1126/science.277.5326.693;
RA Dickens M., Rogers J.S., Cavanagh J., Raitano A., Xia Z., Halpern J.R.,
RA Greenberg M.E., Sawyers C.L., Davis R.J.;
RT "A cytoplasmic inhibitor of the JNK signal transduction pathway.";
RL Science 277:693-696(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JIP-1B; JIP-1C; JIP-1D AND JIP-1E).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10098834; DOI=10.1046/j.1471-4159.1999.721335.x;
RA Kim I.-J., Lee K.-W., Park B.Y., Lee J.-K., Park J., Choi I.Y., Eom S.-J.,
RA Chang T.-S., Kim M.J., Yeom Y.I., Chang S.K., Lee Y.-D., Choi E.-J.,
RA Han P.-L.;
RT "Molecular cloning of multiple splicing variants of JIP-1 preferentially
RT expressed in brain.";
RL J. Neurochem. 72:1335-1343(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10490659; DOI=10.1128/mcb.19.10.7245;
RA Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.;
RT "The JIP group of mitogen-activated protein kinase scaffold proteins.";
RL Mol. Cell. Biol. 19:7245-7254(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND VARIANT ARG-10.
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B).
RC TISSUE=Brain;
RX PubMed=11912189; DOI=10.1074/jbc.m108372200;
RA Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.;
RT "Interaction of Alzheimer's beta-amyloid precursor family proteins with
RT scaffold proteins of the JNK signaling cascade.";
RL J. Biol. Chem. 277:20070-20078(2002).
RN [6]
RP INTERACTION WITH ARHGEF28, AND SUBCELLULAR LOCATION.
RX PubMed=10574993; DOI=10.1074/jbc.274.49.35113;
RA Meyer D., Liu A., Margolis B.;
RT "Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190
RT rhoGEF and its localization in differentiated neurons.";
RL J. Biol. Chem. 274:35113-35118(1999).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10712642; DOI=10.1046/j.1460-9568.2000.00945.x;
RA Pellet J.-B., Haefliger J.-A., Staple J.K., Widmann C., Welker E.,
RA Hirling H., Bonny C., Nicod P., Catsicas S., Waeber G., Riederer B.M.;
RT "Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a
RT homologue of JIP-1, in mouse brain.";
RL Eur. J. Neurosci. 12:621-632(2000).
RN [8]
RP INTERACTION WITH LRPS.
RX PubMed=10827173; DOI=10.1074/jbc.m000955200;
RA Gotthardt M., Trommsdorff M., Nevitt M.F., Shelton J., Richardson J.A.,
RA Stockinger W., Nimpf J., Herz J.;
RT "Interactions of the low density lipoprotein receptor gene family with
RT cytosolic adaptor and scaffold proteins suggest diverse biological
RT functions in cellular communication and signal transduction.";
RL J. Biol. Chem. 275:25616-25624(2000).
RN [9]
RP INTERACTION WITH KLC1.
RC TISSUE=Brain;
RX PubMed=11238452; DOI=10.1083/jcb.152.5.959;
RA Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J., Rapoport T.A.,
RA Margolis B.;
RT "Cargo of kinesin identified as JIP scaffolding proteins and associated
RT signaling molecules.";
RL J. Cell Biol. 152:959-970(2001).
RN [10]
RP FUNCTION.
RX PubMed=11562351; DOI=10.1101/gad.922801;
RA Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
RA Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A., Rakic P.,
RA Davis R.J.;
RT "Requirement of the JIP1 scaffold protein for stress-induced JNK
RT activation.";
RL Genes Dev. 15:2421-2432(2001).
RN [11]
RP INTERACTION WITH DCLK2.
RX PubMed=16628014; DOI=10.4161/cc.5.9.2715;
RA Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
RA Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
RT "Common and divergent roles for members of the mouse DCX superfamily.";
RL Cell Cycle 5:976-983(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-28, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, INTERACTION WITH SH3RF1, AND IDENTIFICATION IN A COMPLEX WITH
RP SH3RF1; RAC1; MAP3K11; MAPK8 AND MAP2K7.
RX PubMed=23963642; DOI=10.1002/eji.201343635;
RA Cunningham C.A., Knudson K.M., Peng B.J., Teixeiro E., Daniels M.A.;
RT "The POSH/JIP-1 scaffold network regulates TCR-mediated JNK1 signals and
RT effector function in CD8(+) T cells.";
RL Eur. J. Immunol. 43:3361-3371(2013).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8; MAP2K7 AND
RP MAPK9.
RX PubMed=27084103; DOI=10.4049/jimmunol.1501728;
RA Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
RT "POSH regulates CD4+ T cell differentiation and survival.";
RL J. Immunol. 196:4003-4013(2016).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module. Required
CC for JNK activation in response to excitotoxic stress. Cytoplasmic
CC MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK
CC in the cytoplasm and thus inhibiting the JNK phosphorylation of c-Jun.
CC May also participate in ApoER2-specific reelin signaling. Directly, or
CC indirectly, regulates GLUT2 gene expression and beta-cell function.
CC Appears to have a role in cell signaling in mature and developing nerve
CC terminals. May function as a regulator of vesicle transport, through
CC interactions with the JNK-signaling components and motor proteins.
CC Functions as an anti-apoptotic protein and whose level seems to
CC influence the beta-cell death or survival response (By similarity).
CC Acts as a scaffold protein that coordinates with SH3RF1 in organizing
CC different components of the JNK pathway, including RAC1 or RAC2,
CC MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2
CC into a functional multiprotein complex to ensure the effective
CC activation of the JNK signaling pathway. Regulates the activation of
CC MAPK8/JNK1 and differentiation of CD8(+) T-cells (PubMed:23963642).
CC {ECO:0000250, ECO:0000269|PubMed:11562351,
CC ECO:0000269|PubMed:23963642}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific
CC components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2,
CC MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and DLK1. Also binds the
CC proline-rich domain-containing splice variant of apolipoprotein E
CC receptor 2 (ApoER2) (By similarity). Binds the cytoplasmic tails of
CC LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of
CC kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes
CC are then transported as a cargo of kinesin, to the required subcellular
CC location. Interacts with the cytoplasmic domain of APP (By similarity).
CC Interacts, via the PID domain, with ARHGEF28. Interacts with
CC MAP3K7/TAK1 and VRK2 (By similarity). Interacts with DCLK2
CC (PubMed:16628014). Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3,
CC MAP2K7/MKK7 and MAPK8/JNK1 (PubMed:23963642). Found in a complex with
CC SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and MAPK9/JNK2
CC (PubMed:27084103). Interacts with SH3RF2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9R237, ECO:0000250|UniProtKB:Q9UQF2,
CC ECO:0000269|PubMed:10574993, ECO:0000269|PubMed:10827173,
CC ECO:0000269|PubMed:11238452, ECO:0000269|PubMed:16628014,
CC ECO:0000269|PubMed:23963642, ECO:0000269|PubMed:27084103}.
CC -!- INTERACTION:
CC Q9WVI9; Q91ZX7: Lrp1; NbExp=2; IntAct=EBI-74515, EBI-300955;
CC Q9WVI9; A2ARV4: Lrp2; NbExp=2; IntAct=EBI-74515, EBI-300875;
CC Q9WVI9-1; P12023: App; NbExp=3; IntAct=EBI-288461, EBI-78814;
CC Q9WVI9-1; P12023-2: App; NbExp=2; IntAct=EBI-288461, EBI-286828;
CC Q9WVI9-1; Q9JI18: Lrp1b; NbExp=3; IntAct=EBI-288461, EBI-8294317;
CC Q9WVI9-1; P45983: MAPK8; Xeno; NbExp=2; IntAct=EBI-288461, EBI-286483;
CC Q9WVI9-2; Q62073: Map3k7; NbExp=4; IntAct=EBI-288464, EBI-1775345;
CC Q9WVI9-2; Q86Y07-2: VRK2; Xeno; NbExp=2; IntAct=EBI-288464, EBI-1207636;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}.
CC Note=Accumulates in cell surface projections. Under certain stress
CC conditions, translocates to the perinuclear region of neurons. In
CC insulin-secreting cells, detected in both the cytoplasm and nucleus (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=JIP-1b;
CC IsoId=Q9WVI9-1; Sequence=Displayed;
CC Name=JIP-1a; Synonyms=1;
CC IsoId=Q9WVI9-2; Sequence=VSP_002766;
CC Name=JIP-1c; Synonyms=2a;
CC IsoId=Q9WVI9-3; Sequence=VSP_002763;
CC Name=JIP-1d; Synonyms=2B;
CC IsoId=Q9WVI9-4; Sequence=VSP_002763, VSP_002765;
CC Name=JIP-1e; Synonyms=3;
CC IsoId=Q9WVI9-5; Sequence=VSP_002764;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brain and insulin-
CC secreting cells. In the brain, high expression found in the cerebral
CC cortex and hippocampus. Localizes in the synaptic regions of the
CC olfactory bulb, retina, cerebral and cerebellar cortex and hippocampus.
CC Also expressed in a restricted number of axons, including mossy fibers
CC from the hippocampal dentate gyrus, soma, dendrites and axons of
CC cerebellar Purkinje cells. Also expressed in kidney, testis and
CC prostate. Low levels in heart, ovary and small intestine. Isoform JIP-
CC 1b is more predominant in the brain than isoform JIP-1a. Isoform Jip1-a
CC is expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-
CC 1d and isoform JIP-1e are brain specific.
CC {ECO:0000269|PubMed:10712642}.
CC -!- DEVELOPMENTAL STAGE: Low levels at prenatal stage 15 dpc, increased
CC levels during the first postnatal days, with a plateau at postnatal day
CC 15.
CC -!- INDUCTION: Upon neuron differentiation.
CC -!- DOMAIN: The SH3 domain mediates homodimerization. {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-
CC 103 is also necessary for the dissociation and activation of MAP3K12.
CC Phosphorylated by VRK2. Hyperphosphorylated during mitosis following
CC activation of stress-activated and MAP kinases (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Two preliminary events are required to prime for
CC ubiquitination; phosphorylation and an increased in intracellular
CC calcium concentration. Then, the calcium influx initiates
CC ubiquitination and degradation by the ubiquitin-proteasome pathway.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF003115; AAB66317.1; -; mRNA.
DR EMBL; AF109768; AAD38346.1; -; mRNA.
DR EMBL; AF109769; AAD38347.1; -; mRNA.
DR EMBL; AF109770; AAD38348.1; -; mRNA.
DR EMBL; AF109771; AAD38349.1; -; mRNA.
DR EMBL; AF054611; AAD22580.1; -; mRNA.
DR EMBL; AF332075; AAK56103.1; -; mRNA.
DR EMBL; AF332076; AAK56104.1; -; mRNA.
DR CCDS; CCDS16446.1; -. [Q9WVI9-1]
DR CCDS; CCDS57180.1; -. [Q9WVI9-3]
DR PIR; T03038; T03038.
DR RefSeq; NP_035292.2; NM_011162.5. [Q9WVI9-1]
DR PDB; 1UKH; X-ray; 2.35 A; B=153-163.
DR PDB; 1UKI; X-ray; 2.70 A; B=153-163.
DR PDB; 3O17; X-ray; 3.00 A; F/G=154-163.
DR PDB; 3O2M; X-ray; 2.70 A; F/G=154-163.
DR PDB; 3V3V; X-ray; 2.70 A; B=153-163.
DR PDB; 6F5E; X-ray; 2.70 A; C=153-163.
DR PDBsum; 1UKH; -.
DR PDBsum; 1UKI; -.
DR PDBsum; 3O17; -.
DR PDBsum; 3O2M; -.
DR PDBsum; 3V3V; -.
DR PDBsum; 6F5E; -.
DR AlphaFoldDB; Q9WVI9; -.
DR SMR; Q9WVI9; -.
DR BioGRID; 202375; 9.
DR IntAct; Q9WVI9; 16.
DR MINT; Q9WVI9; -.
DR STRING; 10090.ENSMUSP00000050773; -.
DR iPTMnet; Q9WVI9; -.
DR PhosphoSitePlus; Q9WVI9; -.
DR MaxQB; Q9WVI9; -.
DR PaxDb; Q9WVI9; -.
DR PeptideAtlas; Q9WVI9; -.
DR PRIDE; Q9WVI9; -.
DR ProteomicsDB; 269421; -. [Q9WVI9-1]
DR ProteomicsDB; 269422; -. [Q9WVI9-2]
DR ProteomicsDB; 269423; -. [Q9WVI9-3]
DR ProteomicsDB; 269424; -. [Q9WVI9-4]
DR ProteomicsDB; 269425; -. [Q9WVI9-5]
DR Antibodypedia; 26197; 291 antibodies from 33 providers.
DR DNASU; 19099; -.
DR Ensembl; ENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223. [Q9WVI9-1]
DR Ensembl; ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223. [Q9WVI9-3]
DR GeneID; 19099; -.
DR KEGG; mmu:19099; -.
DR UCSC; uc008kxv.2; mouse. [Q9WVI9-3]
DR UCSC; uc008kxw.2; mouse. [Q9WVI9-4]
DR UCSC; uc008kxx.2; mouse. [Q9WVI9-1]
DR CTD; 9479; -.
DR MGI; MGI:1309464; Mapk8ip1.
DR VEuPathDB; HostDB:ENSMUSG00000027223; -.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000157089; -.
DR HOGENOM; CLU_006711_1_1_1; -.
DR InParanoid; Q9WVI9; -.
DR OMA; GHHRERI; -.
DR OrthoDB; 372907at2759; -.
DR PhylomeDB; Q9WVI9; -.
DR TreeFam; TF325073; -.
DR BioGRID-ORCS; 19099; 0 hits in 73 CRISPR screens.
DR EvolutionaryTrace; Q9WVI9; -.
DR PRO; PR:Q9WVI9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WVI9; protein.
DR Bgee; ENSMUSG00000027223; Expressed in superior frontal gyrus and 228 other tissues.
DR Genevisible; Q9WVI9; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI.
DR GO; GO:0044302; C:dentate gyrus mossy fiber; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:MGI.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
DR CDD; cd11943; SH3_JIP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50056; -.
DR InterPro; IPR035638; JIP1_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..707
FT /note="C-Jun-amino-terminal kinase-interacting protein 1"
FT /id="PRO_0000220629"
FT DOMAIN 484..545
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 557..696
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..281
FT /note="JNK-binding domain (JBD)"
FT REGION 153..172
FT /note="Minimal inhibitory domain (MID)"
FT REGION 279..467
FT /note="Interaction with MAP3K7"
FT /evidence="ECO:0000250"
FT REGION 425..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..656
FT /note="Interaction with VRK2"
FT /evidence="ECO:0000250"
FT MOTIF 349..356
FT /note="D-box 1"
FT MOTIF 360..368
FT /note="D-box 2"
FT COMPBIAS 102..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 103
FT /note="Phosphothreonine; by MAPK8, MAPK9 and MAPK10"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 201
FT /note="Phosphothreonine; by MAPK8, MAPK9 and MAPK10"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF2"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform JIP-1e)"
FT /evidence="ECO:0000303|PubMed:10098834"
FT /id="VSP_002764"
FT VAR_SEQ 1..33
FT /note="MAERESGLGGGAASPPAASPFLGLHIASPPNFR -> MQLVLKMDSSPDNDS
FT WLEDQWEHW (in isoform JIP-1c and isoform JIP-1d)"
FT /evidence="ECO:0000303|PubMed:10098834"
FT /id="VSP_002763"
FT VAR_SEQ 69..93
FT /note="Missing (in isoform JIP-1d)"
FT /evidence="ECO:0000303|PubMed:10098834"
FT /id="VSP_002765"
FT VAR_SEQ 558..604
FT /note="Missing (in isoform JIP-1a)"
FT /evidence="ECO:0000303|PubMed:9235893"
FT /id="VSP_002766"
FT VARIANT 10
FT /note="G -> R (in strain: ILS)"
FT /evidence="ECO:0000269|PubMed:11471062"
FT CONFLICT 144..145
FT /note="PG -> A (in Ref. 2; AAD38346/AAD38347/AAD38348)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="R -> RP (in Ref. 2; AAD38346/AAD38347/AAD38348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 77282 MW; 274013B12D91049D CRC64;
MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ
CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ
RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK
KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ
MAPPSGPPAT APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE
SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG SLGEPPPPPR
ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS DESDSATVYD NCASASSPYE
SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI
NGEEHEQTHR AIFRFVPRHE DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA
IEVTKEPEHM AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN
PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN KYFGFITKHP
ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP TEDIYLE
