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Q9WVI9 (JIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

Short name=JIP-1
Short name=JNK-interacting protein 1
Alternative name(s):
Islet-brain-1
Short name=IB-1
JNK MAP kinase scaffold protein 1
Mitogen-activated protein kinase 8-interacting protein 1
Gene names
Name:Mapk8ip1
Synonyms:Ib1, Jip1, Mapk8ip, Prkm8ip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length707 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. 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 interactions 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. Ref.1 Ref.10

Subunit structure

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 ARHGEF28. Interacts with MAP3K7 and VRK2 By similarity. Interacts with DCLK2. Ref.6 Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity. Endoplasmic reticulum membrane By similarity. Mitochondrion membrane 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. Ref.6 Ref.7

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-ais expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform JIP-1e are brain specific. Ref.7

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.

Domain

The SH3 domain mediates homodimerization By similarity.

Post-translational modification

Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12. Phosphorylated by VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases By similarity.

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.

Sequence similarities

Belongs to the JIP scaffold family.

Contains 1 PID domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJUN phosphorylation

Inferred from direct assay Ref.1. Source: MGI

negative regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway

Inferred from direct assay Ref.2. Source: MGI

positive regulation of signal transduction

Non-traceable author statement Ref.10. Source: GOC

regulation of JNK cascade

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: MGI

signal transduction

Inferred from direct assay Ref.1. Source: MGI

vesicle-mediated transport

Inferred from direct assay PubMed 16301330. Source: MGI

   Cellular_componentaxon

Inferred from direct assay Ref.7. Source: MGI

axonal growth cone

Inferred from sequence orthology Ref.7. Source: MGI

cell body

Inferred from direct assay Ref.7. Source: MGI

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytosol

Inferred from direct assay Ref.7. Source: MGI

dendrite

Inferred from direct assay Ref.7. Source: MGI

dendritic growth cone

Inferred from sequence orthology Ref.7. Source: MGI

dentate gyrus mossy fiber

Inferred from direct assay Ref.7. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay Ref.7. Source: UniProtKB

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from direct assay PubMed 16301330. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from direct assay Ref.7. Source: MGI

   Molecular_functionMAP-kinase scaffold activity

Non-traceable author statement Ref.10. Source: UniProtKB

kinesin binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 11517249PubMed 19071120PubMed 17709393PubMed 18286207. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform JIP-1b (identifier: Q9WVI9-1)

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 JIP-1a (identifier: Q9WVI9-2)

Also known as: 1;

The sequence of this isoform differs from the canonical sequence as follows:
     558-604: Missing.
Isoform JIP-1c (identifier: Q9WVI9-3)

Also known as: 2a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW
Isoform JIP-1d (identifier: Q9WVI9-4)

Also known as: 2B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW
     69-93: Missing.
Isoform JIP-1e (identifier: Q9WVI9-5)

Also known as: 3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707C-Jun-amino-terminal kinase-interacting protein 1
PRO_0000220629

Regions

Domain484 – 54562SH3
Domain557 – 696140PID
Region127 – 281155JNK-binding domain (JBD)
Region153 – 17220Minimal inhibitory domain (MID)
Region279 – 467189Interaction with MAP3K7 By similarity
Region467 – 656190Interaction with VRK2 By similarity
Motif349 – 3568D-box 1
Motif360 – 3689D-box 2
Compositional bias41 – 477Asp/Glu-rich (acidic)
Compositional bias107 – 11610Asp/Glu-rich (acidic)
Compositional bias355 – 3595Poly-Pro

Amino acid modifications

Modified residue391Phosphoserine By similarity
Modified residue1031Phosphothreonine; by MAPK8, MAPK9 and MAPK10 By similarity
Modified residue1481Phosphoserine By similarity
Modified residue1771Phosphoserine By similarity
Modified residue1831Phosphoserine By similarity
Modified residue1891Phosphoserine By similarity
Modified residue1911Phosphoserine By similarity
Modified residue1921Phosphoserine By similarity
Modified residue2011Phosphothreonine; by MAPK8, MAPK9 and MAPK10 By similarity
Modified residue2101Phosphoserine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3241Phosphoserine By similarity
Modified residue3261Phosphoserine By similarity
Modified residue3361Phosphoserine By similarity
Modified residue3511Phosphoserine By similarity
Modified residue3621Phosphoserine By similarity
Modified residue3651Phosphoserine By similarity
Modified residue4031Phosphoserine By similarity
Modified residue4051Phosphoserine By similarity
Modified residue4071Phosphothreonine By similarity
Modified residue4401Phosphoserine By similarity
Modified residue4431Phosphoserine By similarity
Modified residue4441Phosphothreonine By similarity
Modified residue4651Phosphoserine By similarity
Modified residue4671Phosphoserine By similarity
Modified residue4681Phosphoserine By similarity
Modified residue4691Phosphoserine By similarity

Natural variations

Alternative sequence1 – 9090Missing in isoform JIP-1e.
VSP_002764
Alternative sequence1 – 3333MAERE…PPNFR → MQLVLKMDSSPDNDSWLEDQ WEHW in isoform JIP-1c and isoform JIP-1d.
VSP_002763
Alternative sequence69 – 9325Missing in isoform JIP-1d.
VSP_002765
Alternative sequence558 – 60447Missing in isoform JIP-1a.
VSP_002766
Natural variant101G → R in strain: ILS. Ref.4

Experimental info

Sequence conflict144 – 1452PG → A in AAD38346. Ref.2
Sequence conflict144 – 1452PG → A in AAD38347. Ref.2
Sequence conflict144 – 1452PG → A in AAD38348. Ref.2
Sequence conflict5931R → RP in AAD38346. Ref.2
Sequence conflict5931R → RP in AAD38347. Ref.2
Sequence conflict5931R → RP in AAD38348. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform JIP-1b [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 274013B12D91049D

FASTA70777,282
        10         20         30         40         50         60 
MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ 

        70         80         90        100        110        120 
CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ 

       130        140        150        160        170        180 
RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK 

       190        200        210        220        230        240 
KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ 

       250        260        270        280        290        300 
MAPPSGPPAT APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE 

       310        320        330        340        350        360 
SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG SLGEPPPPPR 

       370        380        390        400        410        420 
ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS DESDSATVYD NCASASSPYE 

       430        440        450        460        470        480 
SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI 

       490        500        510        520        530        540 
NGEEHEQTHR AIFRFVPRHE DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA 

       550        560        570        580        590        600 
IEVTKEPEHM AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN 

       610        620        630        640        650        660 
PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN KYFGFITKHP 

       670        680        690        700 
ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP TEDIYLE 

« Hide

Isoform JIP-1a (1) [UniParc].

Checksum: A303DB4A3C9A9775
Show »

FASTA66071,927
Isoform JIP-1c (2a) [UniParc].

Checksum: 7451CE05C930E9F7
Show »

FASTA69877,009
Isoform JIP-1d (2B) [UniParc].

Checksum: CCB2C92E28D27E23
Show »

FASTA67374,585
Isoform JIP-1e (3) [UniParc].

Checksum: A22DC803C3DB62DF
Show »

FASTA61768,005

References

[1]"A cytoplasmic inhibitor of the JNK signal transduction pathway."
Dickens M., Rogers J.S., Cavanagh J., Raitano A., Xia Z., Halpern J.R., Greenberg M.E., Sawyers C.L., Davis R.J.
Science 277:693-696(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1A), POSSIBLE FUNCTION.
Tissue: Brain.
[2]"Molecular cloning of multiple splicing variants of JIP-1 preferentially expressed in brain."
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.
J. Neurochem. 72:1335-1343(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JIP-1B; JIP-1C; JIP-1D AND JIP-1E).
Strain: BALB/c.
Tissue: Brain.
[3]"The JIP group of mitogen-activated protein kinase scaffold proteins."
Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.
Mol. Cell. Biol. 19:7245-7254(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), CHARACTERIZATION.
Tissue: Brain.
[4]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
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.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), VARIANT ARG-10.
Strain: ILS and ISS.
[5]"Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade."
Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.
J. Biol. Chem. 277:20070-20078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B).
Tissue: Brain.
[6]"Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons."
Meyer D., Liu A., Margolis B.
J. Biol. Chem. 274:35113-35118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF28, SUBCELLULAR LOCATION.
[7]"Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain."
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.
Eur. J. Neurosci. 12:621-632(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]"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."
Gotthardt M., Trommsdorff M., Nevitt M.F., Shelton J., Richardson J.A., Stockinger W., Nimpf J., Herz J.
J. Biol. Chem. 275:25616-25624(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRPS.
[9]"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 KLC1.
Tissue: Brain.
[10]"Requirement of the JIP1 scaffold protein for stress-induced JNK activation."
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.
Genes Dev. 15:2421-2432(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Common and divergent roles for members of the mouse DCX superfamily."
Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T., Brody Y., Orr I., Barkai N., Eichele G., Reiner O.
Cell Cycle 5:976-983(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLK2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF003115 mRNA. Translation: AAB66317.1.
AF109768 mRNA. Translation: AAD38346.1.
AF109769 mRNA. Translation: AAD38347.1.
AF109770 mRNA. Translation: AAD38348.1.
AF109771 mRNA. Translation: AAD38349.1.
AF054611 mRNA. Translation: AAD22580.1.
AF332075 mRNA. Translation: AAK56103.1.
AF332076 mRNA. Translation: AAK56104.1.
CCDSCCDS16446.1. [Q9WVI9-1]
CCDS57180.1. [Q9WVI9-3]
PIRT03038.
RefSeqNP_035292.2. NM_011162.5. [Q9WVI9-1]
UniGeneMm.2720.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKHX-ray2.35B153-163[»]
1UKIX-ray2.70B153-163[»]
3O17X-ray3.00F/G154-163[»]
3O2MX-ray2.70F/G154-163[»]
3V3VX-ray2.70B153-163[»]
ProteinModelPortalQ9WVI9.
SMRQ9WVI9. Positions 486-545.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202375. 4 interactions.
IntActQ9WVI9. 17 interactions.
MINTMINT-126863.
STRING10090.ENSMUSP00000050773.

PTM databases

PhosphoSiteQ9WVI9.

Proteomic databases

PaxDbQ9WVI9.
PRIDEQ9WVI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223. [Q9WVI9-1]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223. [Q9WVI9-3]
GeneID19099.
KEGGmmu:19099.
UCSCuc008kxw.2. mouse. [Q9WVI9-4]
uc008kxx.2. mouse. [Q9WVI9-1]

Organism-specific databases

CTD9479.
MGIMGI:1309464. Mapk8ip1.

Phylogenomic databases

eggNOGNOG266073.
GeneTreeENSGT00390000003908.
HOVERGENHBG018568.
InParanoidQ9WVI9.
KOK04434.
OMASPCRRSA.
OrthoDBEOG74J97M.
PhylomeDBQ9WVI9.
TreeFamTF325073.

Gene expression databases

BgeeQ9WVI9.
GenevestigatorQ9WVI9.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00640. PID. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
PROSITEPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WVI9.
NextBio295662.
PROQ9WVI9.
SOURCESearch...

Entry information

Entry nameJIP1_MOUSE
AccessionPrimary (citable) accession number: Q9WVI9
Secondary accession number(s): O35145 expand/collapse secondary AC list , Q925J8, Q9R1H9, Q9R1Z1, Q9WVI7, Q9WVI8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: July 9, 2014
This is version 143 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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