Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UQF2

- JIP1_HUMAN

UniProt

Q9UQF2 - JIP1_HUMAN

Protein

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

Gene

MAPK8IP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 inhibiting 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 By similarity. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. JUN phosphorylation Source: Ensembl
    2. negative regulation of apoptotic process Source: Ensembl
    3. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    4. negative regulation of JNK cascade Source: Ensembl
    5. negative regulation of JUN kinase activity Source: Ensembl
    6. positive regulation of signal transduction Source: GOC
    7. regulation of JNK cascade Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: Ensembl
    9. vesicle-mediated transport Source: UniProtKB

    Enzyme and pathway databases

    SignaLinkiQ9UQF2.

    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, PRKM8IP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6882. MAPK8IP1.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity. Endoplasmic reticulum membrane. Mitochondrion membrane
    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. axonal growth cone Source: Ensembl
    2. cell body Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Ensembl
    5. dendritic growth cone Source: Ensembl
    6. dentate gyrus mossy fiber Source: Ensembl
    7. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    8. mitochondrial membrane Source: UniProtKB-SubCell
    9. nucleus Source: UniProtKB-SubCell
    10. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    11. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591S → N in NIDDM. 1 Publication
    VAR_012243

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi160 – 1601R → G: Abolishes MAPK9 interaction. 2 Publications
    Mutagenesisi161 – 1611P → G: Abolishes MAPK9 interaction. 2 Publications
    Mutagenesisi704 – 7041P → A: No effect on KNS2 binding. 1 Publication
    Mutagenesisi709 – 7091Y → A: Abolishes KNS2 binding. 1 Publication

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation

    Organism-specific databases

    MIMi125853. phenotype.
    PharmGKBiPA30626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711C-Jun-amino-terminal kinase-interacting protein 1PRO_0000220628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401Phosphoserine2 Publications
    Modified residuei103 – 1031Phosphothreonine; by MAPK8, MAPK9 and MAPK102 Publications
    Modified residuei152 – 1521Phosphoserine1 Publication
    Modified residuei181 – 1811Phosphoserine2 Publications
    Modified residuei187 – 1871Phosphoserine2 Publications
    Modified residuei193 – 1931Phosphoserine2 Publications
    Modified residuei195 – 1951Phosphoserine2 Publications
    Modified residuei196 – 1961Phosphoserine2 Publications
    Modified residuei205 – 2051Phosphothreonine; by MAPK8, MAPK9 and MAPK102 Publications
    Modified residuei214 – 2141Phosphoserine2 Publications
    Modified residuei311 – 3111Phosphoserine2 Publications
    Modified residuei328 – 3281Phosphoserine2 Publications
    Modified residuei330 – 3301Phosphoserine2 Publications
    Modified residuei340 – 3401Phosphoserine2 Publications
    Modified residuei355 – 3551Phosphoserine2 Publications
    Modified residuei366 – 3661Phosphoserine2 Publications
    Modified residuei369 – 3691Phosphoserine2 Publications
    Modified residuei407 – 4071Phosphoserine2 Publications
    Modified residuei409 – 4091Phosphoserine2 Publications
    Modified residuei411 – 4111Phosphothreonine2 Publications
    Modified residuei444 – 4441Phosphoserine2 Publications
    Modified residuei447 – 4471Phosphoserine2 Publications
    Modified residuei448 – 4481Phosphothreonine2 Publications
    Modified residuei469 – 4691Phosphoserine2 Publications
    Modified residuei471 – 4711Phosphoserine2 Publications
    Modified residuei472 – 4721Phosphoserine2 Publications
    Modified residuei473 – 4731Phosphoserine2 Publications

    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 isoform 1 and isoform 2 of VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases.1 Publication
    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

    PaxDbiQ9UQF2.
    PRIDEiQ9UQF2.

    PTM databases

    PhosphoSiteiQ9UQF2.

    Expressioni

    Tissue specificityi

    Highly expressed in brain. Expressed in neurons, localizing to neurite tips in differentiating cells. Also expressed in the pancreas, testis and prostate. Low levels in heart, ovary and small intestine. Decreased levels in pancreatic beta cells sensitize cells to IL-1-beta-induced apoptosis.

    Gene expression databases

    ArrayExpressiQ9UQF2.
    BgeeiQ9UQF2.
    CleanExiHS_MAPK8IP1.
    GenevestigatoriQ9UQF2.

    Organism-specific databases

    HPAiCAB013289.

    Interactioni

    Subunit structurei

    Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely, MAPK8, MAPK9, MAPK10, MAPKK7, MLK2, MLK3, MAP3K12 and MAP3K13. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Interacts, via the PID domain, with ARHGEF28. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of KNS2, then the pre-assembled MAPK8IP1 scaffolding complexes are transported as a cargo of kinesin, to the required subcellular location. Interacts with the cytoplasmic domain of APP. Interacts with DCLK2 By similarity. Interacts with MAP3K7. Interacts with isoform 1 and isoform 2 of VRK2.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AppP120232EBI-78404,EBI-78814From a different organism.
    EGFRP005333EBI-78404,EBI-297353
    ERBB2P046263EBI-78404,EBI-641062
    MAP2K7O147335EBI-78404,EBI-492605
    MAP3K7O4331811EBI-78404,EBI-358684
    MAPK8P459837EBI-78404,EBI-286483

    Protein-protein interaction databases

    BioGridi114864. 26 interactions.
    IntActiQ9UQF2. 14 interactions.
    MINTiMINT-111691.
    STRINGi9606.ENSP00000241014.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G01X-ray3.50F/G157-167[»]
    2GMXX-ray3.50F/G157-167[»]
    2H96X-ray3.00F/G157-167[»]
    3OXIX-ray2.20J158-167[»]
    3PTGX-ray2.43J157-167[»]
    3VUDX-ray3.50F157-167[»]
    3VUGX-ray3.24F157-167[»]
    3VUHX-ray2.70F157-167[»]
    3VUIX-ray2.80F157-167[»]
    3VUKX-ray2.95F157-167[»]
    3VULX-ray2.81F157-167[»]
    3VUMX-ray2.69F157-167[»]
    4E73X-ray2.27B158-167[»]
    4G1WX-ray2.45B157-167[»]
    4H39X-ray1.99B158-167[»]
    4HYSX-ray2.42B157-167[»]
    4HYUX-ray2.15B157-167[»]
    4IZYX-ray2.30B157-167[»]
    ProteinModelPortaliQ9UQF2.
    SMRiQ9UQF2. Positions 490-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UQF2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini488 – 54962SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 700140PIDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 285159JNK-binding domain (JBD)Add
    BLAST
    Regioni157 – 17620Minimal inhibitory domain (MID)Add
    BLAST
    Regioni283 – 471189Interaction with MAP3K7Add
    BLAST
    Regioni471 – 660190Interaction with VRK2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi353 – 3608D-box 1
    Motifi364 – 3729D-box 2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 487Asp/Glu-rich (acidic)
    Compositional biasi79 – 846Poly-Gly
    Compositional biasi107 – 11610Asp/Glu-rich (acidic)
    Compositional biasi331 – 3344Poly-Glu
    Compositional biasi359 – 3635Poly-Pro

    Domaini

    The destruction boxes (D-box) may act as recognition signals for degradation via the ubiquitin-proteasome pathway.
    A minimal inhibitory domain prevents pancreatic beta cell apoptosis in vitro, and prevents activation of c-jun by MAPK8, MAPK9 and MAPK10.
    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.
    HOGENOMiHOG000231470.
    HOVERGENiHBG018568.
    InParanoidiQ9UQF2.
    KOiK04434.
    OMAiSPCRRSA.
    OrthoDBiEOG74J97M.
    PhylomeDBiQ9UQF2.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9UQF2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAERESGGLG GGAASPPAAS PFLGLHIASP PNFRLTHDIS LEEFEDEDLS    50
    EITDECGISL QCKDTLSLRP PRAGLLSAGG GGAGSRLQAE MLQMDLIDAT 100
    GDTPGAEDDE EDDDEERAAR RPGAGPPKAE SGQEPASRGQ GQSQGQSQGP 150
    GSGDTYRPKR PTTLNLFPQV PRSQDTLNNN SLGKKHSWQD RVSRSSSPLK 200
    TGEQTPPHEH ICLSDELPPQ SGPAPTTDRG TSTDSPCRRS TATQMAPPGG 250
    PPAAPPGGRG HSHRDRIHYQ ADVRLEATEE IYLTPVQRPP DAAEPTSAFL 300
    PPTESRMSVS SDPDPAAYPS TAGRPHPSIS EEEEGFDCLS SPERAEPPGG 350
    GWRGSLGEPP PPPRASLSSD TSALSYDSVK YTLVVDEHAQ LELVSLRPCF 400
    GDYSDESDSA TVYDNCASVS SPYESAIGEE YEEAPRPQPP ACLSEDSTPD 450
    EPDVHFSKKF LNVFMSGRSR SSSAESFGLF SCIINGEEQE QTHRAIFRFV 500
    PRHEDELELE VDDPLLVELQ AEDYWYEAYN MRTGARGVFP AYYAIEVTKE 550
    PEHMAALAKN SDWVDQFRVK FLGSVQVPYH KGNDVLCAAM QKIATTRRLT 600
    VHFNPPSSCV LEISVRGVKI GVKADDSQEA KGNKCSHFFQ LKNISFCGYH 650
    PKNNKYFGFI TKHPADHRFA CHVFVSEDST KALAESVGRA FQQFYKQFVE 700
    YTCPTEDIYL E 711
    Length:711
    Mass (Da):77,524
    Last modified:May 1, 2000 - v1
    Checksum:i55EA53B30080A751
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591S → N in NIDDM. 1 Publication
    VAR_012243
    Natural varianti322 – 3221A → V.
    Corresponds to variant rs34420676 [ dbSNP | Ensembl ].
    VAR_049664
    Natural varianti353 – 3531R → Q.
    Corresponds to variant rs12295161 [ dbSNP | Ensembl ].
    VAR_049665

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074091 mRNA. Translation: AAD20443.1.
    CH471064 Genomic DNA. Translation: EAW68027.1.
    CH471064 Genomic DNA. Translation: EAW68028.1.
    AF007134 mRNA. Translation: AAC19150.1.
    CCDSiCCDS7916.1.
    RefSeqiNP_005447.1. NM_005456.3.
    UniGeneiHs.234249.

    Genome annotation databases

    EnsembliENST00000241014; ENSP00000241014; ENSG00000121653.
    GeneIDi9479.
    KEGGihsa:9479.
    UCSCiuc001nbr.3. human.

    Polymorphism databases

    DMDMi17433093.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF074091 mRNA. Translation: AAD20443.1 .
    CH471064 Genomic DNA. Translation: EAW68027.1 .
    CH471064 Genomic DNA. Translation: EAW68028.1 .
    AF007134 mRNA. Translation: AAC19150.1 .
    CCDSi CCDS7916.1.
    RefSeqi NP_005447.1. NM_005456.3.
    UniGenei Hs.234249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G01 X-ray 3.50 F/G 157-167 [» ]
    2GMX X-ray 3.50 F/G 157-167 [» ]
    2H96 X-ray 3.00 F/G 157-167 [» ]
    3OXI X-ray 2.20 J 158-167 [» ]
    3PTG X-ray 2.43 J 157-167 [» ]
    3VUD X-ray 3.50 F 157-167 [» ]
    3VUG X-ray 3.24 F 157-167 [» ]
    3VUH X-ray 2.70 F 157-167 [» ]
    3VUI X-ray 2.80 F 157-167 [» ]
    3VUK X-ray 2.95 F 157-167 [» ]
    3VUL X-ray 2.81 F 157-167 [» ]
    3VUM X-ray 2.69 F 157-167 [» ]
    4E73 X-ray 2.27 B 158-167 [» ]
    4G1W X-ray 2.45 B 157-167 [» ]
    4H39 X-ray 1.99 B 158-167 [» ]
    4HYS X-ray 2.42 B 157-167 [» ]
    4HYU X-ray 2.15 B 157-167 [» ]
    4IZY X-ray 2.30 B 157-167 [» ]
    ProteinModelPortali Q9UQF2.
    SMRi Q9UQF2. Positions 490-549.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114864. 26 interactions.
    IntActi Q9UQF2. 14 interactions.
    MINTi MINT-111691.
    STRINGi 9606.ENSP00000241014.

    PTM databases

    PhosphoSitei Q9UQF2.

    Polymorphism databases

    DMDMi 17433093.

    Proteomic databases

    PaxDbi Q9UQF2.
    PRIDEi Q9UQF2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000241014 ; ENSP00000241014 ; ENSG00000121653 .
    GeneIDi 9479.
    KEGGi hsa:9479.
    UCSCi uc001nbr.3. human.

    Organism-specific databases

    CTDi 9479.
    GeneCardsi GC11P045908.
    HGNCi HGNC:6882. MAPK8IP1.
    HPAi CAB013289.
    MIMi 125853. phenotype.
    604641. gene.
    neXtProti NX_Q9UQF2.
    PharmGKBi PA30626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266073.
    HOGENOMi HOG000231470.
    HOVERGENi HBG018568.
    InParanoidi Q9UQF2.
    KOi K04434.
    OMAi SPCRRSA.
    OrthoDBi EOG74J97M.
    PhylomeDBi Q9UQF2.
    TreeFami TF325073.

    Enzyme and pathway databases

    SignaLinki Q9UQF2.

    Miscellaneous databases

    ChiTaRSi MAPK8IP1. human.
    EvolutionaryTracei Q9UQF2.
    GeneWikii MAPK8IP1.
    GenomeRNAii 9479.
    NextBioi 35528.
    PROi Q9UQF2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQF2.
    Bgeei Q9UQF2.
    CleanExi HS_MAPK8IP1.
    Genevestigatori Q9UQF2.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00640. PID. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    PROSITEi PS01179. PID. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/C-jun-amino-terminal kinase interacting protein-1 (JIP-1) gene."
      Mooser V., Maillard A., Bonny C., Steinmann M., Shaw P., Yarnall D.P., Burns D.K., Schorderet D.F., Nicod P., Waeber G.
      Genomics 55:202-208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Insulinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Yu W., Sarginson J., Gibbs R.A.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 468-711.
      Tissue: Brain.
    4. "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.
    5. "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: MUTAGENESIS, INTERACTION WITH KINESIN.
    6. "Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase pathway."
      Ikeda A., Hasegawa K., Masaki M., Moriguchi T., Nishida E., Kozutsumi Y., Oka S., Kawasaki T.
      J. Biochem. 130:773-781(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K13.
    7. "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: INTERACTION WITH APP.
    8. "Recruitment of JNK to JIP1 and JNK-dependent JIP1 phosphorylation regulates JNK module dynamics and activation."
      Nihalani D., Wong H.N., Holzman L.B.
      J. Biol. Chem. 278:28694-28702(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-103 AND THR-205, MUTAGENESIS OF ARG-160 AND PRO-161.
    9. "Cell-permeable peptide inhibitors of JNK: novel blockers of beta-cell death."
      Bonny C., Oberson A., Negri S., Sauser C., Schorderet D.F.
      Diabetes 50:77-82(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PEPTIDE INHIBITORS OF JNK.
    10. Cited for: CALCIUM- AND PROTEASOME-DEPENDENT DEGRADATION.
    11. "A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia."
      Borsello T., Clarke P.G., Hirt L., Vercelli A., Repici M., Schorderet D.F., Bogousslavsky J., Bonny C.
      Nat. Med. 9:1180-1186(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTECTION AGAINST EXCITOTOXICITY AND CEREBRAL ISCHEMIA.
    12. "Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease."
      D'Ambrosio C., Arena S., Fulcoli G., Scheinfeld M.H., Zhou D., D'Adamio L., Scaloni A.
      Mol. Cell. Proteomics 5:97-113(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-40; SER-181; SER-187; SER-193; SER-195; SER-196; SER-214; SER-311; SER-328; SER-330; SER-340; SER-355; SER-366; SER-369; SER-407; SER-409; THR-411; SER-444; SER-447; SER-444; THR-448; SER-469; SER-471; SER-472 AND SER-473.
    13. "Vaccinia-related kinase 2 modulates the stress response to hypoxia mediated by TAK1."
      Blanco S., Santos C., Lazo P.A.
      Mol. Cell. Biol. 27:7273-7283(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K7.
    14. "Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
      Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
      PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VRK2, PHOSPHORYLATION.
    15. Cited for: VARIANT NIDDM ASN-59.

    Entry informationi

    Entry nameiJIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQF2
    Secondary accession number(s): D3DQP4, O43407
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    A chemically synthesized cell-permeable peptide of the minimal inhibitory domain decreases brain lesions in both transient and permanent ischemia. The level of protection is still high when administered 6 or 12 hours after ischemia.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3