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Q9UQF2

- JIP1_HUMAN

UniProt

Q9UQF2 - JIP1_HUMAN

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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

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 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
Complete GO annotation...

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 Source: UniProtKB-KW
  8. membrane Source: UniProtKB-KW
  9. mitochondrion Source: UniProtKB-KW
  10. nucleus Source: UniProtKB-KW
  11. perinuclear region of cytoplasm Source: Ensembl
  12. synapse Source: Ensembl
Complete GO annotation...

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. 1 Publication
Mutagenesisi161 – 1611P → G: Abolishes MAPK9 interaction. 1 Publication
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 – 401Phosphoserine1 Publication
Modified residuei103 – 1031Phosphothreonine; by MAPK8, MAPK9 and MAPK101 Publication
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei187 – 1871Phosphoserine1 Publication
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei196 – 1961Phosphoserine1 Publication
Modified residuei205 – 2051Phosphothreonine; by MAPK8, MAPK9 and MAPK101 Publication
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei311 – 3111Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei366 – 3661Phosphoserine1 Publication
Modified residuei369 – 3691Phosphoserine1 Publication
Modified residuei407 – 4071Phosphoserine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei444 – 4441Phosphoserine1 Publication
Modified residuei447 – 4471Phosphoserine1 Publication
Modified residuei448 – 4481Phosphothreonine1 Publication
Modified residuei469 – 4691Phosphoserine1 Publication
Modified residuei471 – 4711Phosphoserine1 Publication
Modified residuei472 – 4721Phosphoserine1 Publication
Modified residuei473 – 4731Phosphoserine1 Publication

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

BgeeiQ9UQF2.
CleanExiHS_MAPK8IP1.
ExpressionAtlasiQ9UQF2. baseline and differential.
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, 556-690.
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.
GeneTreeiENSGT00390000003908.
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

        10         20         30         40         50
MAERESGGLG GGAASPPAAS PFLGLHIASP PNFRLTHDIS LEEFEDEDLS
60 70 80 90 100
EITDECGISL QCKDTLSLRP PRAGLLSAGG GGAGSRLQAE MLQMDLIDAT
110 120 130 140 150
GDTPGAEDDE EDDDEERAAR RPGAGPPKAE SGQEPASRGQ GQSQGQSQGP
160 170 180 190 200
GSGDTYRPKR PTTLNLFPQV PRSQDTLNNN SLGKKHSWQD RVSRSSSPLK
210 220 230 240 250
TGEQTPPHEH ICLSDELPPQ SGPAPTTDRG TSTDSPCRRS TATQMAPPGG
260 270 280 290 300
PPAAPPGGRG HSHRDRIHYQ ADVRLEATEE IYLTPVQRPP DAAEPTSAFL
310 320 330 340 350
PPTESRMSVS SDPDPAAYPS TAGRPHPSIS EEEEGFDCLS SPERAEPPGG
360 370 380 390 400
GWRGSLGEPP PPPRASLSSD TSALSYDSVK YTLVVDEHAQ LELVSLRPCF
410 420 430 440 450
GDYSDESDSA TVYDNCASVS SPYESAIGEE YEEAPRPQPP ACLSEDSTPD
460 470 480 490 500
EPDVHFSKKF LNVFMSGRSR SSSAESFGLF SCIINGEEQE QTHRAIFRFV
510 520 530 540 550
PRHEDELELE VDDPLLVELQ AEDYWYEAYN MRTGARGVFP AYYAIEVTKE
560 570 580 590 600
PEHMAALAKN SDWVDQFRVK FLGSVQVPYH KGNDVLCAAM QKIATTRRLT
610 620 630 640 650
VHFNPPSSCV LEISVRGVKI GVKADDSQEA KGNKCSHFFQ LKNISFCGYH
660 670 680 690 700
PKNNKYFGFI TKHPADHRFA CHVFVSEDST KALAESVGRA FQQFYKQFVE
710
YTCPTEDIYL E
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, 556-690.
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.
GeneTreei ENSGT00390000003908.
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

Bgeei Q9UQF2.
CleanExi HS_MAPK8IP1.
ExpressionAtlasi Q9UQF2. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 142 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