Q13387 · JIP2_HUMAN
- ProteinC-Jun-amino-terminal kinase-interacting protein 2
- GeneMAPK8IP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids824 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameC-Jun-amino-terminal kinase-interacting protein 2
- Short namesJIP-2; JNK-interacting protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13387
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Accumulates in cell surface projections.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_049666 | 743 | in dbSNP:rs1140555 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 942 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000220631 | 1-824 | UniProt | C-Jun-amino-terminal kinase-interacting protein 2 | |||
Sequence: MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEDEEEEEEEEEGDGEGQEGGDPGSEAPAPGPLIPSPSVEEPHKHRPTTLRLTTLGAQDSLNNNGGFDLVRPASWQETALCSPAPEALRELPGPLPATDTGPGGAQSPVRPGCDCEGNRPAEPPAPGGTSPSSDPGIEADLRSRSSGGRGGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSSGRSSHLTNSIEEASSPASEPEPPREPPRRPAFLPVGPDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRPPGEPVSPAGGAAQDSQDPEAAAGPGGVELVDMETLCAPPPPAPAAPRPGPAQPGPCLFLSNPTRDTITPLWAAPGRAARPGRACSAACSEEEDEEDDEEEEDAEDSAGSPGGRGTGPSAPRDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLGHDSEEDSGGEASEEEAGAALLGGGQVSGDTSPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCLVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVERFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVAQSVGRAFLEYYQEHLAYACPTEDIYLE | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 254 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 254 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 302 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 305 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed mainly in the brain and pancreas, including insulin-secreting cells. In the nervous system, more abundantly expressed in the cerebellum, pituitary gland, occipital lobe and the amygdala. Also expressed in fetal brain. Very low levels found in uterus, ovary, prostate, colon, testis, adrenal gland, thyroid gland and salivary gland.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely JNK1, JNK2, JNK3, MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). 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 (By similarity).
Interacts with the cytoplasmic domain of APP (By similarity).
Interacts with DCLK2. Interacts with TIAM1 and TIAM2 (By similarity).
Interacts with FGF13; enables the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding activity. Interacts with SH3RF2 (By similarity).
Interacts with the cytoplasmic domain of APP (By similarity).
Interacts with DCLK2. Interacts with TIAM1 and TIAM2 (By similarity).
Interacts with FGF13; enables the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding activity. Interacts with SH3RF2 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13387 | ANGPT1 Q15389-2 | 3 | EBI-722813, EBI-10692491 | |
BINARY | Q13387 | EGFR P00533 | 5 | EBI-722813, EBI-297353 | |
BINARY | Q13387 | ERBB2 P04626 | 3 | EBI-722813, EBI-641062 | |
BINARY | Q13387 | Q53HF2 | 2 | EBI-722813, EBI-877761 | |
BINARY | Q13387 | UBD O15205 | 3 | EBI-722813, EBI-6657186 | |
BINARY | Q13387-4 | CAMK2A Q9UQM7 | 3 | EBI-12345753, EBI-1383687 | |
BINARY | Q13387-4 | CASP1 P29466-3 | 3 | EBI-12345753, EBI-12248206 | |
BINARY | Q13387-4 | GFAP P14136 | 3 | EBI-12345753, EBI-744302 | |
BINARY | Q13387-4 | HOXC8 P31273 | 3 | EBI-12345753, EBI-1752118 | |
BINARY | Q13387-4 | ITGB1 P05556 | 3 | EBI-12345753, EBI-703066 | |
BINARY | Q13387-4 | PIK3R1 P27986-2 | 3 | EBI-12345753, EBI-9090282 | |
BINARY | Q13387-4 | PRKACA P17612 | 3 | EBI-12345753, EBI-476586 | |
BINARY | Q13387-4 | RAC1 P63000 | 3 | EBI-12345753, EBI-413628 | |
BINARY | Q13387-4 | SDC2 P34741 | 3 | EBI-12345753, EBI-1172957 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MADRAEMFSLSTFHSLSPPGCRPPQDIS | ||||||
Region | 40-160 | Disordered | ||||
Sequence: ITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEDEEEEEEEEEGDGEGQEGGDPGSEAPAPGPLIPSPSVEEPHKHRPTTLRLTTLGAQDSLNNNGGFDL | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: SYDSDHCEKDSLSLG | ||||||
Compositional bias | 79-110 | Acidic residues | ||||
Sequence: QEFEMIDDNEEEDDEDEEEEEEEEEGDGEGQE | ||||||
Region | 110-275 | JNK-binding domain (JBD) | ||||
Sequence: EGGDPGSEAPAPGPLIPSPSVEEPHKHRPTTLRLTTLGAQDSLNNNGGFDLVRPASWQETALCSPAPEALRELPGPLPATDTGPGGAQSPVRPGCDCEGNRPAEPPAPGGTSPSSDPGIEADLRSRSSGGRGGRRSSQELSSPGSDSEDAGGARLGRMISSISETE | ||||||
Compositional bias | 142-160 | Polar residues | ||||
Sequence: RLTTLGAQDSLNNNGGFDL | ||||||
Region | 172-349 | Disordered | ||||
Sequence: CSPAPEALRELPGPLPATDTGPGGAQSPVRPGCDCEGNRPAEPPAPGGTSPSSDPGIEADLRSRSSGGRGGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSSGRSSHLTNSIEEASSPASEPEPPREPPRRPAFLPVGPDDTNSEYESGSESEPDLSEDADSPW | ||||||
Compositional bias | 239-254 | Polar residues | ||||
Sequence: GRGGRRSSQELSSPGS | ||||||
Region | 239-498 | Necessary for interaction with FGF13 | ||||
Sequence: GRGGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSSGRSSHLTNSIEEASSPASEPEPPREPPRRPAFLPVGPDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRPPGEPVSPAGGAAQDSQDPEAAAGPGGVELVDMETLCAPPPPAPAAPRPGPAQPGPCLFLSNPTRDTITPLWAAPGRAARPGRACSAACSEEEDEEDDEEEEDAEDSAGSPGGRGTGPSA | ||||||
Compositional bias | 272-302 | Polar residues | ||||
Sequence: SETELELSSDGGSSSSGRSSHLTNSIEEASS | ||||||
Region | 361-501 | Disordered | ||||
Sequence: EGSSPIRCPGQCLSPAPRPPGEPVSPAGGAAQDSQDPEAAAGPGGVELVDMETLCAPPPPAPAAPRPGPAQPGPCLFLSNPTRDTITPLWAAPGRAARPGRACSAACSEEEDEEDDEEEEDAEDSAGSPGGRGTGPSAPRD | ||||||
Compositional bias | 415-434 | Pro residues | ||||
Sequence: CAPPPPAPAAPRPGPAQPGP | ||||||
Compositional bias | 468-484 | Acidic residues | ||||
Sequence: SEEEDEEDDEEEEDAED | ||||||
Domain | 604-665 | SH3 | ||||
Sequence: EREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPG | ||||||
Domain | 677-813 | PID | ||||
Sequence: PCWVERFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVAQSVGRAFLEYYQEHLA |
Sequence similarities
Belongs to the JIP scaffold family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.
Q13387-1
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.
- Name1
- Length824
- Mass (Da)87,975
- Last updated2001-12-05 v2
- Checksum7EFC8F3BC58E37BB
Q13387-2
- Name2
- Differences from canonical
- 1-57: MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEK → MLPDFPSPSTWAPGLLLPSGPALLSPSVLQ
Q13387-3
- Name3
- NoteMight be artifactual as it is only predicted from a genomic sequence.
Q13387-4
- Name4
- Differences from canonical
- 88-468: Missing
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002770 | 1-57 | in isoform 2 and isoform 3 | |||
Sequence: MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEK → MLPDFPSPSTWAPGLLLPSGPALLSPSVLQ | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: SYDSDHCEKDSLSLG | ||||||
Compositional bias | 79-110 | Acidic residues | ||||
Sequence: QEFEMIDDNEEEDDEDEEEEEEEEEGDGEGQE | ||||||
Alternative sequence | VSP_002771 | 88-468 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 142-160 | Polar residues | ||||
Sequence: RLTTLGAQDSLNNNGGFDL | ||||||
Alternative sequence | VSP_002772 | 152-394 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 239-254 | Polar residues | ||||
Sequence: GRGGRRSSQELSSPGS | ||||||
Compositional bias | 272-302 | Polar residues | ||||
Sequence: SETELELSSDGGSSSSGRSSHLTNSIEEASS | ||||||
Compositional bias | 415-434 | Pro residues | ||||
Sequence: CAPPPPAPAAPRPGPAQPGP | ||||||
Alternative sequence | VSP_002773 | 415-439 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 468-484 | Acidic residues | ||||
Sequence: SEEEDEEDDEEEEDAED | ||||||
Alternative sequence | VSP_002774 | 768 | in isoform 3 | |||
Sequence: C → CEAPQGAAFQWERGVDRKRVLQTRGNVQPHLGAGQGAALNRATEGSSTGSEKGEWTPLVIMELTQSVNSC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF136382 EMBL· GenBank· DDBJ | AAF00980.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218778 EMBL· GenBank· DDBJ | AAF32323.1 EMBL· GenBank· DDBJ | mRNA | ||
U62317 EMBL· GenBank· DDBJ | AAB03340.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC009940 EMBL· GenBank· DDBJ | AAH09940.2 EMBL· GenBank· DDBJ | mRNA | ||
AL021708 EMBL· GenBank· DDBJ | CAA16714.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U79261 EMBL· GenBank· DDBJ | AAB50207.1 EMBL· GenBank· DDBJ | mRNA |