JIP3_MOUSE
ID JIP3_MOUSE Reviewed; 1337 AA.
AC Q9ESN9; Q5D062; Q99KU7; Q9EQD8; Q9ESN7; Q9ESN8; Q9ESP0; Q9JLH2; Q9JLH3;
AC Q9R0U7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 3;
DE Short=JIP-3;
DE Short=JNK-interacting protein 3;
DE AltName: Full=JNK MAP kinase scaffold protein 3;
DE AltName: Full=JNK/SAPK-associated protein 1;
DE Short=JSAP1;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 3;
DE AltName: Full=Sunday driver 2;
GN Name=Mapk8ip3; Synonyms=Jip3, Jsap1, Syd2;
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 {ECO:0000312|EMBL:BAB16675.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, PHOSPHORYLATION, AND
RP INTERACTION WITH MAPK8; MAPK9; MAPK10; MAP2K4 AND MAP3K1.
RC TISSUE=Brain;
RX PubMed=10523642; DOI=10.1128/mcb.19.11.7539;
RA Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K.,
RA Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that
RT functions as a scaffold factor in the JNK signaling pathway.";
RL Mol. Cell. Biol. 19:7539-7548(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A; 1B; 1C; 1D AND 1E), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11024282; DOI=10.1016/s0378-1119(00)00335-8;
RA Ito M., Akechi M., Hirose R., Ichimura M., Takamatsu N., Xu P.,
RA Nakabeppu Y., Tadayoshi S., Yamamoto K., Yoshioka K.;
RT "Isoforms of JSAP1 scaffold protein generated through alternative
RT splicing.";
RL Gene 255:229-234(2000).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1C AND 3A), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-266; THR-276 AND
RP THR-287, MUTAGENESIS OF ARG-205; PRO-206; THR-207; SER-208; LEU-209;
RP THR-266; THR-276 AND THR-287, AND INTERACTION WITH MAPK8IP2; MAPK8; MAPK9;
RP MAPK10; MAP2K7 AND MAP3K11.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Heart;
RX PubMed=10629060; DOI=10.1128/mcb.20.3.1030-1043.2000;
RA Kelkar N., Gupta S., Dickens M., Davis R.J.;
RT "Interaction of a mitogen-activated protein kinase signaling module with
RT the neuronal protein JIP3.";
RL Mol. Cell. Biol. 20:1030-1043(2000).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH KLC1.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11106729; DOI=10.1016/s0092-8674(00)00162-8;
RA Bowman A.B., Kamal A., Ritchings B.W., Philp A.V., McGrail M.,
RA Gindhart J.G., Goldstein L.S.B.;
RT "Kinesin-dependent axonal transport is mediated by the Sunday Driver (SYD)
RT protein.";
RL Cell 103:583-594(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1240-1337 (ISOFORM 1C).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305}
RP INTERACTION WITH KLC.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287; SER-366 AND SER-603, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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 [9]
RP INTERACTION WITH NTRK2 AND NTRK3.
RX PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011;
RA Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J.,
RA Chen Z.Y.;
RT "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
RT signaling by directly bridging TrkB with kinesin-1.";
RL J. Neurosci. 31:10602-10614(2011).
RN [10]
RP FUNCTION, AND DOMAINS KBD; JBD AND LZ.
RX PubMed=23576431; DOI=10.1074/jbc.m113.464453;
RA Sun T., Yu N., Zhai L.K., Li N., Zhang C., Zhou L., Huang Z., Jiang X.Y.,
RA Shen Y., Chen Z.Y.;
RT "c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates
RT neuronal axon elongation in a kinesin- and JNK-dependent manner.";
RL J. Biol. Chem. 288:14531-14543(2013).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25944905; DOI=10.1074/jbc.m115.651885;
RA Watt D., Dixit R., Cavalli V.;
RT "JIP3 activates kinesin-1 motility to promote axon elongation.";
RL J. Biol. Chem. 290:15512-15525(2015).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=28259553; DOI=10.1016/j.bbrc.2017.02.132;
RA Ma H., Yu H., Li T., Zhao Y., Hou M., Chen Z., Wang Y., Sun T.;
RT "JIP3 regulates neuronal radial migration by mediating TrkB axonal
RT anterograde transport in the developing cerebral cortex.";
RL Biochem. Biophys. Res. Commun. 485:790-795(2017).
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. May
CC function as a regulator of vesicle transport, through interactions with
CC the JNK-signaling components and motor proteins (PubMed:10523642,
CC PubMed:10629060). Promotes neuronal axon elongation in a kinesin- and
CC JNK-dependent manner (PubMed:23576431, PubMed:25944905,
CC PubMed:28259553). Activates cofilin at axon tips via local activation
CC of JNK, thereby regulating filopodial dynamics and enhancing axon
CC elongation (PubMed:23576431, PubMed:25944905, PubMed:28259553). Its
CC binding to kinesin heavy chains (KHC), promotes kinesin-1 motility
CC along microtubules and is essential for axon elongation and
CC regeneration (PubMed:23576431, PubMed:25944905, PubMed:28259553).
CC Regulates cortical neuronal migration by mediating NTRK2/TRKB
CC anterograde axonal transport during brain development (PubMed:23576431,
CC PubMed:25944905, PubMed:28259553). Acts as an adapter that bridges the
CC interaction between NTRK2/TRKB and KLC1 and drives NTRK2/TRKB axonal
CC but not dendritic anterograde transport, which is essential for
CC subsequent BDNF-triggered signaling and filopodia formation
CC (PubMed:23576431, PubMed:25944905, PubMed:28259553).
CC {ECO:0000269|PubMed:10523642, ECO:0000269|PubMed:10629060,
CC ECO:0000269|PubMed:23576431, ECO:0000269|PubMed:25944905,
CC ECO:0000269|PubMed:28259553}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes. The central region
CC of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but not MAPK8IP1.
CC Binds specific components of the JNK signaling pathway namely
CC MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-terminal region,
CC MAP2K4/MKK4 and MAP2K7/MKK7 to the central region and MAP3K11 to the C-
CC terminal region. Binds the TPR motif-containing C-terminal of kinesin
CC light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are
CC then transported as a cargo of kinesin, to the required subcellular
CC location (PubMed:10523642, PubMed:10629060, PubMed:11238452,
CC PubMed:11106729). Interacts with ROCK1 and this interaction is enhanced
CC by ultraviolet-B (UVB) radiation. Interacts with SH3RF2 (By
CC similarity). Interacts with NTRK2/TRKB and NTRK3/TRKC
CC (PubMed:21775604). {ECO:0000250|UniProtKB:E9PSK7,
CC ECO:0000250|UniProtKB:Q9UPT6, ECO:0000269|PubMed:10523642,
CC ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729,
CC ECO:0000269|PubMed:11238452, ECO:0000269|PubMed:21775604}.
CC -!- INTERACTION:
CC Q9ESN9; P62331: Arf6; NbExp=8; IntAct=EBI-301496, EBI-988682;
CC Q9ESN9; P28738: Kif5c; NbExp=8; IntAct=EBI-301496, EBI-2506834;
CC Q9ESN9; O88447: Klc1; NbExp=9; IntAct=EBI-301496, EBI-301550;
CC Q9ESN9; O88448: Klc2; NbExp=6; IntAct=EBI-301496, EBI-301558;
CC Q9ESN9-2; P31938: Map2k1; NbExp=3; IntAct=EBI-9549291, EBI-298860;
CC Q9ESN9-2; P47809: Map2k4; NbExp=3; IntAct=EBI-9549291, EBI-447934;
CC Q9ESN9-2; P53349: Map3k1; NbExp=3; IntAct=EBI-9549291, EBI-447913;
CC Q9ESN9-2; Q61831: Mapk10; NbExp=4; IntAct=EBI-9549291, EBI-400741;
CC Q9ESN9-2; P04049: RAF1; Xeno; NbExp=2; IntAct=EBI-9549291, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10629060}. Golgi
CC apparatus {ECO:0000269|PubMed:11106729}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11106729}. Cell projection, growth cone
CC {ECO:0000269|PubMed:10629060}. Cell projection, axon
CC {ECO:0000269|PubMed:25944905}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:E9PSK7}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:E9PSK7}. Note=Localized in the soma and growth
CC cones of differentiated neurites and the Golgi and vesicles of the
CC early secretory compartment of epithelial cells (PubMed:10629060,
CC PubMed:11106729). KIF5A/B/C-mediated transportation to axon tips is
CC essential for its function in enhancing neuronal axon elongation (By
CC similarity). {ECO:0000250|UniProtKB:E9PSK7,
CC ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:11106729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1c; Synonyms=3b;
CC IsoId=Q9ESN9-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=Q9ESN9-2; Sequence=VSP_002775, VSP_002777;
CC Name=1b;
CC IsoId=Q9ESN9-3; Sequence=VSP_002776, VSP_002777;
CC Name=1d;
CC IsoId=Q9ESN9-4; Sequence=VSP_002775;
CC Name=3a;
CC IsoId=Q9ESN9-5; Sequence=VSP_002778, VSP_002779;
CC Name=1e;
CC IsoId=Q9ESN9-6; Sequence=VSP_002776;
CC -!- TISSUE SPECIFICITY: Highly expressed throughout many regions of the
CC brain and at lower levels in the heart, liver, lung, testes and kidney.
CC All isoforms have been identified in the brain, isoform 1a is also
CC expressed in the spleen and lung. {ECO:0000269|PubMed:10629060,
CC ECO:0000269|PubMed:11024282}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the brain of embryonic mice.
CC Expression levels gradually increase from 10 dpc to postnatal day 10
CC (P10) (at protein level). {ECO:0000269|PubMed:28259553}.
CC -!- INDUCTION: Expressed in neurites 5 days following initiation of nerve
CC growth factor induced differentiation. NGF withdrawal results in the
CC down-regulation of MAPK8IP3 protein by caspase-mediated cleavage.
CC {ECO:0000269|PubMed:10629060}.
CC -!- PTM: Phosphorylation by ROCK1 is crucial for the recruitment of JNK.
CC {ECO:0000250|UniProtKB:Q9UPT6}.
CC -!- DISRUPTION PHENOTYPE: The cerebral cortex in the embryonic brain is a
CC little thinner and the distribution of neurons is more disordered than
CC that found in the wild-type littermates. {ECO:0000269|PubMed:28259553}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG36931.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB005662; BAA85874.1; -; mRNA.
DR EMBL; AB043124; BAB16675.1; -; mRNA.
DR EMBL; AB043125; BAB16676.1; -; mRNA.
DR EMBL; AB043123; BAB16674.1; -; mRNA.
DR EMBL; AB043129; BAB16685.1; -; Genomic_DNA.
DR EMBL; AF178637; AAF26843.1; -; mRNA.
DR EMBL; AF178636; AAF26842.1; -; mRNA.
DR EMBL; AF262046; AAG36931.1; ALT_INIT; mRNA.
DR EMBL; BC004003; AAH04003.1; -; mRNA.
DR EMBL; BC060603; AAH60603.1; -; mRNA.
DR CCDS; CCDS37498.1; -. [Q9ESN9-1]
DR CCDS; CCDS50024.1; -. [Q9ESN9-4]
DR CCDS; CCDS50025.1; -. [Q9ESN9-5]
DR CCDS; CCDS50026.1; -. [Q9ESN9-2]
DR CCDS; CCDS50029.1; -. [Q9ESN9-3]
DR RefSeq; NP_001156919.1; NM_001163447.1. [Q9ESN9-4]
DR RefSeq; NP_001156920.1; NM_001163448.1. [Q9ESN9-5]
DR RefSeq; NP_001156921.1; NM_001163449.1. [Q9ESN9-3]
DR RefSeq; NP_001156923.1; NM_001163451.1. [Q9ESN9-2]
DR RefSeq; NP_038959.2; NM_013931.4. [Q9ESN9-1]
DR PDB; 6EJN; X-ray; 3.20 A; C/D=417-486.
DR PDBsum; 6EJN; -.
DR AlphaFoldDB; Q9ESN9; -.
DR SMR; Q9ESN9; -.
DR BioGRID; 206033; 11.
DR IntAct; Q9ESN9; 18.
DR MINT; Q9ESN9; -.
DR STRING; 10090.ENSMUSP00000085683; -.
DR GlyConnect; 2216; 1 N-Linked glycan (1 site).
DR GlyGen; Q9ESN9; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9ESN9; -.
DR PhosphoSitePlus; Q9ESN9; -.
DR EPD; Q9ESN9; -.
DR MaxQB; Q9ESN9; -.
DR PaxDb; Q9ESN9; -.
DR PeptideAtlas; Q9ESN9; -.
DR PRIDE; Q9ESN9; -.
DR ProteomicsDB; 269028; -. [Q9ESN9-1]
DR ProteomicsDB; 269029; -. [Q9ESN9-2]
DR ProteomicsDB; 269030; -. [Q9ESN9-3]
DR ProteomicsDB; 269031; -. [Q9ESN9-4]
DR ProteomicsDB; 269032; -. [Q9ESN9-5]
DR ProteomicsDB; 269033; -. [Q9ESN9-6]
DR Antibodypedia; 3958; 166 antibodies from 34 providers.
DR DNASU; 30957; -.
DR Ensembl; ENSMUST00000088345; ENSMUSP00000085683; ENSMUSG00000024163. [Q9ESN9-1]
DR Ensembl; ENSMUST00000115228; ENSMUSP00000110883; ENSMUSG00000024163. [Q9ESN9-5]
DR Ensembl; ENSMUST00000117509; ENSMUSP00000112712; ENSMUSG00000024163. [Q9ESN9-3]
DR Ensembl; ENSMUST00000119115; ENSMUSP00000112955; ENSMUSG00000024163. [Q9ESN9-2]
DR Ensembl; ENSMUST00000120035; ENSMUSP00000114084; ENSMUSG00000024163. [Q9ESN9-4]
DR Ensembl; ENSMUST00000146923; ENSMUSP00000114802; ENSMUSG00000024163. [Q9ESN9-1]
DR GeneID; 30957; -.
DR KEGG; mmu:30957; -.
DR UCSC; uc008aza.2; mouse. [Q9ESN9-5]
DR UCSC; uc008azb.2; mouse. [Q9ESN9-1]
DR UCSC; uc008azc.2; mouse. [Q9ESN9-3]
DR UCSC; uc008aze.2; mouse. [Q9ESN9-2]
DR UCSC; uc008azf.2; mouse. [Q9ESN9-4]
DR CTD; 23162; -.
DR MGI; MGI:1353598; Mapk8ip3.
DR VEuPathDB; HostDB:ENSMUSG00000024163; -.
DR eggNOG; KOG2077; Eukaryota.
DR GeneTree; ENSGT00940000153496; -.
DR InParanoid; Q9ESN9; -.
DR PhylomeDB; Q9ESN9; -.
DR TreeFam; TF313096; -.
DR BioGRID-ORCS; 30957; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mapk8ip3; mouse.
DR PRO; PR:Q9ESN9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9ESN9; protein.
DR Bgee; ENSMUSG00000024163; Expressed in dentate gyrus of hippocampal formation granule cell and 254 other tissues.
DR ExpressionAtlas; Q9ESN9; baseline and differential.
DR Genevisible; Q9ESN9; MM.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR GO; GO:0008432; F:JUN kinase binding; IPI:BHF-UCL.
DR GO; GO:0019894; F:kinesin binding; IDA:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:BHF-UCL.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:BHF-UCL.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:BHF-UCL.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0031103; P:axon regeneration; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1337
FT /note="C-Jun-amino-terminal kinase-interacting protein 3"
FT /id="PRO_0000220634"
FT DOMAIN 12..100
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 521..595
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 50..80
FT /note="Kinesin-binding domain (KBD); essential for its
FT function in axon elongation"
FT /evidence="ECO:0000269|PubMed:23576431"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..226
FT /note="JNK-binding domain (JBD); essential for its function
FT in axon elongation"
FT /evidence="ECO:0000269|PubMed:23576431"
FT REGION 245..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..459
FT /note="Leucine zipper-like domain (LZ); essential for its
FT function in axon elongation"
FT /evidence="ECO:0000269|PubMed:23576431"
FT REGION 459..515
FT /note="Interaction with NTRK2"
FT /evidence="ECO:0000269|PubMed:21775604"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..177
FT /evidence="ECO:0000255"
FT COILED 437..555
FT /evidence="ECO:0000255"
FT COMPBIAS 634..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10629060"
FT MOD_RES 276
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10629060"
FT MOD_RES 287
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:10629060,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPT6"
FT MOD_RES 365
FT /note="Phosphoserine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:Q9UPT6"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT VAR_SEQ 201
FT /note="Missing (in isoform 1a and isoform 1d)"
FT /evidence="ECO:0000303|PubMed:10523642"
FT /id="VSP_002775"
FT VAR_SEQ 201
FT /note="S -> SPRQSWRKS (in isoform 1b and isoform 1e)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002776"
FT VAR_SEQ 219..249
FT /note="Missing (in isoform 1a and isoform 1b)"
FT /evidence="ECO:0000303|PubMed:10523642,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_002777"
FT VAR_SEQ 410..415
FT /note="Missing (in isoform 3a)"
FT /evidence="ECO:0000305"
FT /id="VSP_002778"
FT VAR_SEQ 505..513
FT /note="Missing (in isoform 3a)"
FT /evidence="ECO:0000305"
FT /id="VSP_002779"
FT MUTAGEN 205
FT /note="R->G: Results in inhibition of JNK binding."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 206
FT /note="P->G: Results in inhibition of JNK binding."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 207
FT /note="T->G: Results in inhibition of JNK binding."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 208
FT /note="S->G: Results in inhibition of JNK binding."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 209
FT /note="L->G: Results in inhibition of JNK binding."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 266
FT /note="T->A: Results in loss of phosphorylation of
FT MAPK8IP3; when associated with A-276 and A-287. Does not
FT effect binding of components of the JNK pathway."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 276
FT /note="T->A: Results in loss of phosphorylation of
FT MAPK8IP3; when associated with A-266 and A-287. Does not
FT effect binding of components of the JNK pathway."
FT /evidence="ECO:0000269|PubMed:10629060"
FT MUTAGEN 287
FT /note="T->A: Results in loss of phosphorylation of
FT MAPK8IP3; when associated with A-266 and A-287. Does not
FT effect binding of components of the JNK pathway."
FT /evidence="ECO:0000269|PubMed:10629060"
FT CONFLICT 312
FT /note="K -> R (in Ref. 4; AAG36931)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="F -> L (in Ref. 3; AAF26843)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="E -> K (in Ref. 4; AAG36931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="A -> V (in Ref. 4; AAG36931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="A -> D (in Ref. 4; AAG36931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="S -> T (in Ref. 4; AAG36931)"
FT /evidence="ECO:0000305"
FT HELIX 417..474
FT /evidence="ECO:0007829|PDB:6EJN"
SQ SEQUENCE 1337 AA; 147561 MW; D7DEE54C17B74106 CRC64;
MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
RSKMQQVGGS GQTESSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG
QLQSSSSYQC PNDEMSESGQ SSAAATPSTT GTKSNTPTSS VPSAAVTPLN ESLQPLGDYV
SVTKNNKQAR EKRNSRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDVCPETRL
ERTGSSPTQG IVNKAFGINT DSLYHELSTA GSEVIGDVDE GADLLGEFSV RDDFFGMGKE
VGNLLLENSQ LLETKNALNV VKNDLIAKVD QLSGEQEVLK GELEAAKQAK VKLENRIKEL
EEELKRVKSE AVTARREPRE EVEDVSSYLC TELDKIPMAQ RRRFTRVEMA RVLMERNQYK
ERLMELQEAV RWTEMIRASR EHPSVQEKKK STIWQFFSRL FSSSSSPPPA KRSYPSVNIH
YKSPTAAGFS QRRSHALCQI SAGSRPLEFF PDDDCTSSAR REQKREQYRQ VREHVRNDDG
RLQACGWSLP AKYKQLSPNG GQEDTRMKNV PVPVYCRPLV EKDPSTKLWC AAGVNLSGWK
PHEEDSSNGP KPVPGRDPLT CDREGEGEPK STHPSPEKKK AKETPEADAT SSRVWILTST
LTTSKVVIID ANQPGTIVDQ FTVCNAHVLC ISSIPAASDS DYPPGEMFLD SDVNPEDSGA
DGVLAGITLV GCATRCNVPR SNCSSRGDTP VLDKGQGDVA TTANGKVNPS QSTEEATEAT
EVPDPGPSES EATTVRPGPL TEHVFTDPAP TPSSSTQPAS ENGSESNGTI VQPQVEPSGE
LSTTTSSAAP TMWLGAQNGW LYVHSAVANW KKCLHSIKLK DSVLSLVHVK GRVLVALADG
TLAIFHRGED GQWDLSNYHL MDLGHPHHSI RCMAVVNDRV WCGYKNKVHV IQPKTMQIEK
SFDAHPRRES QVRQLAWIGD GVWVSIRLDS TLRLYHAHTH QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LLIAGNRLWV GTGNGVVISI PLTETVVLHR GQLLGLRANK TSPTSGEGTR
PGGIIHVYGD DSSDKAASSF IPYCSMAQAQ LCFHGHRDAV KFFVSVPGNV LATLNGSVLD
SPSEGPGPAA PAADAEGQKL KNALVLSGGE GYIDFRIGDG EDDETEECAG DVNQTKPSLS
KAERSHIIVW QVSYTPE
