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Protein

C-Jun-amino-terminal kinase-interacting protein 1

Gene

Mapk8ip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. kinesin binding Source: UniProtKB
  2. MAP-kinase scaffold activity Source: UniProtKB
  3. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. JUN phosphorylation Source: MGI
  2. negative regulation of intrinsic apoptotic signaling pathway Source: MGI
  3. negative regulation of JUN kinase activity Source: Ensembl
  4. regulation of JNK cascade Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: MGI
  6. signal transduction Source: MGI
  7. vesicle-mediated transport Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Mapk8ip1
Synonyms:Ib1, Jip1, Mapk8ip, Prkm8ip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1309464. Mapk8ip1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. axon Source: MGI
  2. axonal growth cone Source: MGI
  3. cell body Source: MGI
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: MGI
  6. dendrite Source: MGI
  7. dendritic growth cone Source: MGI
  8. dentate gyrus mossy fiber Source: MGI
  9. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  10. membrane Source: UniProtKB
  11. mitochondrial membrane Source: UniProtKB-SubCell
  12. neuron projection Source: MGI
  13. nucleus Source: UniProtKB-SubCell
  14. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  15. synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707707C-Jun-amino-terminal kinase-interacting protein 1PRO_0000220629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei103 – 1031Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity
Modified residuei148 – 1481PhosphoserineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei201 – 2011Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei336 – 3361PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity
Modified residuei362 – 3621PhosphoserineBy similarity
Modified residuei365 – 3651PhosphoserineBy similarity
Modified residuei403 – 4031PhosphoserineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei407 – 4071PhosphothreonineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity
Modified residuei443 – 4431PhosphoserineBy similarity
Modified residuei444 – 4441PhosphothreonineBy similarity
Modified residuei465 – 4651PhosphoserineBy similarity
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei468 – 4681PhosphoserineBy similarity
Modified residuei469 – 4691PhosphoserineBy similarity

Post-translational modificationi

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).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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9WVI9.
PaxDbiQ9WVI9.
PRIDEiQ9WVI9.

PTM databases

PhosphoSiteiQ9WVI9.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Low levels at prenatal stage E15, increased levels during the first postnatal days, with a plateau at postnatal day 15.

Inductioni

Upon neuron differentiation.

Gene expression databases

BgeeiQ9WVI9.
GenevestigatoriQ9WVI9.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AppP120233EBI-288461,EBI-78814
AppP12023-22EBI-288461,EBI-286828
Lrp1Q91ZX72EBI-74515,EBI-300955
Lrp1bQ9JI183EBI-288461,EBI-8294317
Lrp2A2ARV42EBI-74515,EBI-300875
Map3k7Q620734EBI-288464,EBI-1775345
MAPK8P459832EBI-288461,EBI-286483From a different organism.
VRK2Q86Y07-22EBI-288464,EBI-1207636From a different organism.

Protein-protein interaction databases

BioGridi202375. 4 interactions.
IntActiQ9WVI9. 17 interactions.
MINTiMINT-126863.
STRINGi10090.ENSMUSP00000050773.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9WVI9.
SMRiQ9WVI9. Positions 486-686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WVI9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini484 – 54562SH3PROSITE-ProRule annotationAdd
BLAST
Domaini557 – 696140PIDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 281155JNK-binding domain (JBD)Add
BLAST
Regioni153 – 17220Minimal inhibitory domain (MID)Add
BLAST
Regioni279 – 467189Interaction with MAP3K7By similarityAdd
BLAST
Regioni467 – 656190Interaction with VRK2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi349 – 3568D-box 1
Motifi360 – 3689D-box 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 477Asp/Glu-rich (acidic)
Compositional biasi107 – 11610Asp/Glu-rich (acidic)
Compositional biasi355 – 3595Poly-Pro

Domaini

The SH3 domain mediates homodimerization.By similarity

Sequence similaritiesi

Belongs to the JIP scaffold family.Curated
Contains 1 PID domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG266073.
GeneTreeiENSGT00390000003908.
HOVERGENiHBG018568.
InParanoidiQ9WVI9.
KOiK04434.
OMAiSPCRRSA.
OrthoDBiEOG74J97M.
PhylomeDBiQ9WVI9.
TreeFamiTF325073.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00640. PID. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform JIP-1b (identifier: Q9WVI9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE
60 70 80 90 100
ITDECGISLQ CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA
110 120 130 140 150
GDTPGAEDDE EEEDDELAAQ RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD
160 170 180 190 200
TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK KHSWQDRVSR SSSPLKTGEQ
210 220 230 240 250
TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ MAPPSGPPAT
260 270 280 290 300
APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE
310 320 330 340 350
SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG
360 370 380 390 400
SLGEPPPPPR ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS
410 420 430 440 450
DESDSATVYD NCASASSPYE SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV
460 470 480 490 500
HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI NGEEHEQTHR AIFRFVPRHE
510 520 530 540 550
DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA IEVTKEPEHM
560 570 580 590 600
AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN
610 620 630 640 650
PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN
660 670 680 690 700
KYFGFITKHP ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP

TEDIYLE
Length:707
Mass (Da):77,282
Last modified:December 5, 2001 - v2
Checksum:i274013B12D91049D
GO
Isoform JIP-1a (identifier: Q9WVI9-2) [UniParc]FASTAAdd to Basket

Also known as: 1

The sequence of this isoform differs from the canonical sequence as follows:
     558-604: Missing.

Show »
Length:660
Mass (Da):71,927
Checksum:iA303DB4A3C9A9775
GO
Isoform JIP-1c (identifier: Q9WVI9-3) [UniParc]FASTAAdd to Basket

Also known as: 2a

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW

Show »
Length:698
Mass (Da):77,009
Checksum:i7451CE05C930E9F7
GO
Isoform JIP-1d (identifier: Q9WVI9-4) [UniParc]FASTAAdd to Basket

Also known as: 2B

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW
     69-93: Missing.

Show »
Length:673
Mass (Da):74,585
Checksum:iCCB2C92E28D27E23
GO
Isoform JIP-1e (identifier: Q9WVI9-5) [UniParc]FASTAAdd to Basket

Also known as: 3

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

Show »
Length:617
Mass (Da):68,005
Checksum:iA22DC803C3DB62DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1452PG → A in AAD38346. (PubMed:10098834)Curated
Sequence conflicti144 – 1452PG → A in AAD38347. (PubMed:10098834)Curated
Sequence conflicti144 – 1452PG → A in AAD38348. (PubMed:10098834)Curated
Sequence conflicti593 – 5931R → RP in AAD38346. (PubMed:10098834)Curated
Sequence conflicti593 – 5931R → RP in AAD38347. (PubMed:10098834)Curated
Sequence conflicti593 – 5931R → RP in AAD38348. (PubMed:10098834)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101G → R in strain: ILS. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform JIP-1e. 1 PublicationVSP_002764Add
BLAST
Alternative sequencei1 – 3333MAERE…PPNFR → MQLVLKMDSSPDNDSWLEDQ WEHW in isoform JIP-1c and isoform JIP-1d. 1 PublicationVSP_002763Add
BLAST
Alternative sequencei69 – 9325Missing in isoform JIP-1d. 1 PublicationVSP_002765Add
BLAST
Alternative sequencei558 – 60447Missing in isoform JIP-1a. 1 PublicationVSP_002766Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16446.1. [Q9WVI9-1]
CCDS57180.1. [Q9WVI9-3]
PIRiT03038.
RefSeqiNP_035292.2. NM_011162.5. [Q9WVI9-1]
UniGeneiMm.2720.

Genome annotation databases

EnsembliENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223. [Q9WVI9-1]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223. [Q9WVI9-3]
GeneIDi19099.
KEGGimmu:19099.
UCSCiuc008kxw.2. mouse. [Q9WVI9-4]
uc008kxx.2. mouse. [Q9WVI9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16446.1. [Q9WVI9-1]
CCDS57180.1. [Q9WVI9-3]
PIRiT03038.
RefSeqiNP_035292.2. NM_011162.5. [Q9WVI9-1]
UniGeneiMm.2720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9WVI9.
SMRiQ9WVI9. Positions 486-686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202375. 4 interactions.
IntActiQ9WVI9. 17 interactions.
MINTiMINT-126863.
STRINGi10090.ENSMUSP00000050773.

PTM databases

PhosphoSiteiQ9WVI9.

Proteomic databases

MaxQBiQ9WVI9.
PaxDbiQ9WVI9.
PRIDEiQ9WVI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223. [Q9WVI9-1]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223. [Q9WVI9-3]
GeneIDi19099.
KEGGimmu:19099.
UCSCiuc008kxw.2. mouse. [Q9WVI9-4]
uc008kxx.2. mouse. [Q9WVI9-1]

Organism-specific databases

CTDi9479.
MGIiMGI:1309464. Mapk8ip1.

Phylogenomic databases

eggNOGiNOG266073.
GeneTreeiENSGT00390000003908.
HOVERGENiHBG018568.
InParanoidiQ9WVI9.
KOiK04434.
OMAiSPCRRSA.
OrthoDBiEOG74J97M.
PhylomeDBiQ9WVI9.
TreeFamiTF325073.

Miscellaneous databases

EvolutionaryTraceiQ9WVI9.
NextBioi295662.
PROiQ9WVI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVI9.
GenevestigatoriQ9WVI9.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00640. PID. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. 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. 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.

Entry informationi

Entry nameiJIP1_MOUSE
AccessioniPrimary (citable) accession number: Q9WVI9
Secondary accession number(s): O35145
, Q925J8, Q9R1H9, Q9R1Z1, Q9WVI7, Q9WVI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: January 7, 2015
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.