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Q9ESN9 (JIP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-Jun-amino-terminal kinase-interacting protein 3

Short name=JIP-3
Short name=JNK-interacting protein 3
Alternative name(s):
JNK MAP kinase scaffold protein 3
JNK/SAPK-associated protein 1
Short name=JSAP1
Mitogen-activated protein kinase 8-interacting protein 3
Sunday driver 2
Gene names
Name:Mapk8ip3
Synonyms:Jip3, Jsap1, Syd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Ref.1 Ref.3

Subunit structure

Forms homo- or heterooligomeric complexes. The central region of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but not MAPK8IP1. Binds specific components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-terminal region, MAP2K4/MKK4 and MAP2K7/MKK7 to the central region and MAP3K11 to the C-terminal region. Binds the TPR motif-containing C-terminal of kinesin light chain, pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location. Interacts with ROCK1 and this interaction is enhanced by ultraviolet-B (UVB) radiation By similarity. Ref.1 Ref.3 Ref.4 Ref.6

Subcellular location

Cytoplasm. Golgi apparatus. Cytoplasmic vesicle. Cell projectiongrowth cone. Note: Localized in the soma and growth cones of differentiated neurites and the Golgi and vesicles of the early secretory compartment of epithelial cells. Ref.3 Ref.4

Tissue specificity

Highly expressed throughout many regions of the brain and at lower levels in the heart, liver, lung, testes and kidney. All isoforms have been identified in the brain, isoform 1a is also expressed in the spleen and lung. Ref.2 Ref.3

Induction

Expressed in neurites 5 days following initiation of nerve growth factor induced differentiation. NGF withdrawal results in the down-regulation of MAPK8IP3 protein by caspase-mediated cleavage. Ref.3

Post-translational modification

Phosphorylation by ROCK1 is crucial for the recruitment of JNK By similarity.

Sequence similarities

Belongs to the JIP scaffold family.

Sequence caution

The sequence AAG36931.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from direct assay Ref.3. Source: MGI

activation of JUN kinase activity

Inferred from direct assay PubMed 15767678. Source: MGI

axon guidance

Inferred from mutant phenotype PubMed 15572149. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 12897243PubMed 15572149. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 18324732. Source: MGI

lung alveolus development

Inferred from mutant phenotype PubMed 18324732. Source: MGI

lung morphogenesis

Inferred from mutant phenotype PubMed 18324732. Source: MGI

positive regulation of JUN kinase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from mutant phenotype PubMed 18324732. Source: MGI

protein localization

Inferred from mutant phenotype PubMed 15572149. Source: MGI

regulation of JNK cascade

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of gene expression

Inferred from direct assay PubMed 18324732. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype PubMed 12897243. Source: MGI

vesicle-mediated transport

Inferred from direct assay Ref.4. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from direct assay Ref.4. Source: UniProtKB

axolemma

Inferred from direct assay PubMed 16606357. Source: MGI

cytoplasm

Inferred from direct assay Ref.1. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay PubMed 16606357. Source: MGI

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 16606357. Source: MGI

smooth endoplasmic reticulum

Inferred from direct assay PubMed 16606357. Source: MGI

   Molecular_functionJUN kinase binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

MAP-kinase scaffold activity

Inferred from physical interaction Ref.3. Source: UniProtKB

kinesin binding

Inferred from physical interaction Ref.3. Source: UniProtKB

mitogen-activated protein kinase kinase binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction Ref.1. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1c (identifier: Q9ESN9-1)

Also known as: 3b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1a (identifier: Q9ESN9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     201-201: Missing.
     219-249: Missing.
Isoform 1b (identifier: Q9ESN9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     201-201: S → SPRQSWRKS
     219-249: Missing.
Isoform 1d (identifier: Q9ESN9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     201-201: Missing.
Isoform 3a (identifier: Q9ESN9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     410-415: Missing.
     505-513: Missing.
Isoform 1e (identifier: Q9ESN9-6)

The sequence of this isoform differs from the canonical sequence as follows:
     201-201: S → SPRQSWRKS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13371337C-Jun-amino-terminal kinase-interacting protein 3
PRO_0000220634

Regions

Coiled coil58 – 177120 Potential
Coiled coil437 – 555119 Potential

Amino acid modifications

Modified residue2661Phosphothreonine; by MAPK Ref.1 Ref.3
Modified residue2761Phosphothreonine; by MAPK Ref.1 Ref.3
Modified residue2871Phosphothreonine; by MAPK Ref.1 Ref.3
Modified residue3151Phosphoserine; by ROCK1 By similarity
Modified residue3651Phosphoserine; by ROCK1 By similarity
Modified residue3661Phosphoserine; by ROCK1 By similarity
Modified residue6771Phosphoserine Ref.7

Natural variations

Alternative sequence2011Missing in isoform 1a and isoform 1d. Ref.1 Ref.2
VSP_002775
Alternative sequence2011S → SPRQSWRKS in isoform 1b and isoform 1e. Ref.2
VSP_002776
Alternative sequence219 – 24931Missing in isoform 1a and isoform 1b. Ref.1 Ref.2
VSP_002777
Alternative sequence410 – 4156Missing in isoform 3a. Ref.3
VSP_002778
Alternative sequence505 – 5139Missing in isoform 3a. Ref.3
VSP_002779

Experimental info

Mutagenesis2051R → G: Results in inhibition of JNK binding. Ref.3
Mutagenesis2061P → G: Results in inhibition of JNK binding. Ref.3
Mutagenesis2071T → G: Results in inhibition of JNK binding. Ref.3
Mutagenesis2081S → G: Results in inhibition of JNK binding. Ref.3
Mutagenesis2091L → G: Results in inhibition of JNK binding. Ref.3
Mutagenesis2661T → A: Results in loss of phosphorylation of MAPK8IP3; when associated with A-276 and A-287. Does not effect binding of components of the JNK pathway. Ref.3
Mutagenesis2761T → A: Results in loss of phosphorylation of MAPK8IP3; when associated with A-266 and A-287. Does not effect binding of components of the JNK pathway. Ref.3
Mutagenesis2871T → A: Results in loss of phosphorylation of MAPK8IP3; when associated with A-266 and A-287. Does not effect binding of components of the JNK pathway. Ref.3
Sequence conflict3121K → R in AAG36931. Ref.4
Sequence conflict3761F → L in AAF26843. Ref.3
Sequence conflict5611E → K in AAG36931. Ref.4
Sequence conflict12721A → V in AAG36931. Ref.4
Sequence conflict13221A → D in AAG36931. Ref.4
Sequence conflict13251S → T in AAG36931. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1c (3b) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D7DEE54C17B74106

FASTA1,337147,561
        10         20         30         40         50         60 
MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV 

        70         80         90        100        110        120 
NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK 

       130        140        150        160        170        180 
ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE 

       190        200        210        220        230        240 
RSKMQQVGGS GQTESSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG 

       250        260        270        280        290        300 
QLQSSSSYQC PNDEMSESGQ SSAAATPSTT GTKSNTPTSS VPSAAVTPLN ESLQPLGDYV 

       310        320        330        340        350        360 
SVTKNNKQAR EKRNSRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDVCPETRL 

       370        380        390        400        410        420 
ERTGSSPTQG IVNKAFGINT DSLYHELSTA GSEVIGDVDE GADLLGEFSV RDDFFGMGKE 

       430        440        450        460        470        480 
VGNLLLENSQ LLETKNALNV VKNDLIAKVD QLSGEQEVLK GELEAAKQAK VKLENRIKEL 

       490        500        510        520        530        540 
EEELKRVKSE AVTARREPRE EVEDVSSYLC TELDKIPMAQ RRRFTRVEMA RVLMERNQYK 

       550        560        570        580        590        600 
ERLMELQEAV RWTEMIRASR EHPSVQEKKK STIWQFFSRL FSSSSSPPPA KRSYPSVNIH 

       610        620        630        640        650        660 
YKSPTAAGFS QRRSHALCQI SAGSRPLEFF PDDDCTSSAR REQKREQYRQ VREHVRNDDG 

       670        680        690        700        710        720 
RLQACGWSLP AKYKQLSPNG GQEDTRMKNV PVPVYCRPLV EKDPSTKLWC AAGVNLSGWK 

       730        740        750        760        770        780 
PHEEDSSNGP KPVPGRDPLT CDREGEGEPK STHPSPEKKK AKETPEADAT SSRVWILTST 

       790        800        810        820        830        840 
LTTSKVVIID ANQPGTIVDQ FTVCNAHVLC ISSIPAASDS DYPPGEMFLD SDVNPEDSGA 

       850        860        870        880        890        900 
DGVLAGITLV GCATRCNVPR SNCSSRGDTP VLDKGQGDVA TTANGKVNPS QSTEEATEAT 

       910        920        930        940        950        960 
EVPDPGPSES EATTVRPGPL TEHVFTDPAP TPSSSTQPAS ENGSESNGTI VQPQVEPSGE 

       970        980        990       1000       1010       1020 
LSTTTSSAAP TMWLGAQNGW LYVHSAVANW KKCLHSIKLK DSVLSLVHVK GRVLVALADG 

      1030       1040       1050       1060       1070       1080 
TLAIFHRGED GQWDLSNYHL MDLGHPHHSI RCMAVVNDRV WCGYKNKVHV IQPKTMQIEK 

      1090       1100       1110       1120       1130       1140 
SFDAHPRRES QVRQLAWIGD GVWVSIRLDS TLRLYHAHTH QHLQDVDIEP YVSKMLGTGK 

      1150       1160       1170       1180       1190       1200 
LGFSFVRITA LLIAGNRLWV GTGNGVVISI PLTETVVLHR GQLLGLRANK TSPTSGEGTR 

      1210       1220       1230       1240       1250       1260 
PGGIIHVYGD DSSDKAASSF IPYCSMAQAQ LCFHGHRDAV KFFVSVPGNV LATLNGSVLD 

      1270       1280       1290       1300       1310       1320 
SPSEGPGPAA PAADAEGQKL KNALVLSGGE GYIDFRIGDG EDDETEECAG DVNQTKPSLS 

      1330 
KAERSHIIVW QVSYTPE 

« Hide

Isoform 1a [UniParc].

Checksum: 0BF7257DCFF6D236
Show »

FASTA1,305144,138
Isoform 1b [UniParc].

Checksum: 1EAD24AC1DAD9AB7
Show »

FASTA1,314145,251
Isoform 1d [UniParc].

Checksum: 362061FA2B2AA3C1
Show »

FASTA1,336147,474
Isoform 3a [UniParc].

Checksum: 8C71A02B7FF3FBB4
Show »

FASTA1,322145,785
Isoform 1e [UniParc].

Checksum: AA7157299921450A
Show »

FASTA1,345148,587

References

« Hide 'large scale' references
[1]"JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a scaffold factor in the JNK signaling pathway."
Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.
Mol. Cell. Biol. 19:7539-7548(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, PHOSPHORYLATION, INTERACTION WITH MAPK8; MAPK9; MAPK10; MAP2K4 AND MAP3K1.
Tissue: Brain.
[2]"Isoforms of JSAP1 scaffold protein generated through alternative splicing."
Ito M., Akechi M., Hirose R., Ichimura M., Takamatsu N., Xu P., Nakabeppu Y., Tadayoshi S., Yamamoto K., Yoshioka K.
Gene 255:229-234(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A; 1B; 1C; 1D AND 1E), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3."
Kelkar N., Gupta S., Dickens M., Davis R.J.
Mol. Cell. Biol. 20:1030-1043(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1C AND 3A), FUNCTION, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-266; THR-276 AND THR-287, MUTAGENESIS OF ARG-205; PRO-206; THR-207; SER-208; LEU-209; THR-266; THR-276 AND THR-287, INTERACTION WITH MAPK8IP2; MAPK8; MAPK9; MAPK10; MAP2K7 AND MAP3K11.
Strain: C57BL/6.
Tissue: Brain and Heart.
[4]"Kinesin-dependent axonal transport is mediated by the Sunday Driver (SYD) protein."
Bowman A.B., Kamal A., Ritchings B.W., Philp A.V., McGrail M., Gindhart J.G., Goldstein L.S.B.
Cell 103:583-594(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C), SUBCELLULAR LOCATION, INTERACTION WITH KLC1.
Strain: C57BL/6.
Tissue: Brain.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1240-1337 (ISOFORM 1C).
Strain: C57BL/6.
Tissue: Brain.
[6]"Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules."
Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J., Rapoport T.A., Margolis B.
J. Cell Biol. 152:959-970(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLC.
Tissue: Brain.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005662 mRNA. Translation: BAA85874.1.
AB043124 mRNA. Translation: BAB16675.1.
AB043125 mRNA. Translation: BAB16676.1.
AB043123 mRNA. Translation: BAB16674.1.
AB043129 Genomic DNA. Translation: BAB16685.1.
AF178637 mRNA. Translation: AAF26843.1.
AF178636 mRNA. Translation: AAF26842.1.
AF262046 mRNA. Translation: AAG36931.1. Different initiation.
BC004003 mRNA. Translation: AAH04003.1.
BC060603 mRNA. Translation: AAH60603.1.
RefSeqNP_001156919.1. NM_001163447.1.
NP_001156920.1. NM_001163448.1.
NP_001156921.1. NM_001163449.1.
NP_001156923.1. NM_001163451.1.
NP_038959.2. NM_013931.4.
UniGeneMm.43081.

3D structure databases

ProteinModelPortalQ9ESN9.
SMRQ9ESN9. Positions 417-476, 1049-1105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206033. 6 interactions.
IntActQ9ESN9. 8 interactions.
MINTMINT-7892366.

PTM databases

PhosphoSiteQ9ESN9.

Proteomic databases

PaxDbQ9ESN9.
PRIDEQ9ESN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000088345; ENSMUSP00000085683; ENSMUSG00000024163. [Q9ESN9-1]
ENSMUST00000115228; ENSMUSP00000110883; ENSMUSG00000024163. [Q9ESN9-5]
ENSMUST00000117509; ENSMUSP00000112712; ENSMUSG00000024163. [Q9ESN9-3]
ENSMUST00000119115; ENSMUSP00000112955; ENSMUSG00000024163. [Q9ESN9-2]
ENSMUST00000120035; ENSMUSP00000114084; ENSMUSG00000024163. [Q9ESN9-4]
ENSMUST00000146923; ENSMUSP00000114802; ENSMUSG00000024163. [Q9ESN9-1]
GeneID30957.
KEGGmmu:30957.
UCSCuc008aza.2. mouse. [Q9ESN9-5]
uc008azb.2. mouse. [Q9ESN9-1]
uc008azc.2. mouse. [Q9ESN9-3]
uc008aze.2. mouse. [Q9ESN9-2]
uc008azf.2. mouse. [Q9ESN9-4]

Organism-specific databases

CTD23162.
MGIMGI:1353598. Mapk8ip3.

Phylogenomic databases

eggNOGNOG270333.
GeneTreeENSGT00670000097546.
HOVERGENHBG024110.
KOK04436.
OrthoDBEOG7GXP9P.
PhylomeDBQ9ESN9.
TreeFamTF313096.

Gene expression databases

ArrayExpressQ9ESN9.
BgeeQ9ESN9.
GenevestigatorQ9ESN9.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR019143. JNK/Rab-associated_protein-1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF09744. Jnk-SapK_ap_N. 1 hit.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
ProtoNetSearch...

Other

NextBio307444.
PROQ9ESN9.
SOURCESearch...

Entry information

Entry nameJIP3_MOUSE
AccessionPrimary (citable) accession number: Q9ESN9
Secondary accession number(s): Q5D062 expand/collapse secondary AC list , Q99KU7, Q9EQD8, Q9ESN7, Q9ESN8, Q9ESP0, Q9JLH2, Q9JLH3, Q9R0U7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot