Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

Mapk8ip1

Organism
Rattus norvegicus (Rat)
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

  • identical protein binding Source: IntAct
  • JUN kinase binding Source: RGD
  • kinesin binding Source: UniProtKB
  • MAP-kinase scaffold activity Source: RGD
  • mitogen-activated protein kinase kinase binding Source: RGD
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • JUN phosphorylation Source: Ensembl
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  • negative regulation of JNK cascade Source: RGD
  • negative regulation of JUN kinase activity Source: RGD
  • regulation of JNK cascade Source: UniProtKB
  • regulation of transcription, DNA-templated Source: Ensembl
  • signal transduction Source: RGD
  • vesicle-mediated transport Source: Ensembl
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
JIP-1-related protein
Short name:
JRP
JNK MAP kinase scaffold protein 1
Mitogen-activated protein kinase 8-interacting protein 1
Gene namesi
Name:Mapk8ip1
Synonyms:Ib1, Jip1, Mapk8ip
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi70937. Mapk8ip1.

Subcellular locationi

GO - Cellular componenti

  • axonal growth cone Source: MGI
  • cell body Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • dendritic growth cone Source: MGI
  • dentate gyrus mossy fiber Source: Ensembl
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • mitochondrial membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: RGD
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002206301 – 708C-Jun-amino-terminal kinase-interacting protein 1Add BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Modified residuei39PhosphoserineBy similarity1
Modified residuei103Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity1
Modified residuei149PhosphoserineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei190PhosphoserineBy similarity1
Modified residuei192PhosphoserineBy similarity1
Modified residuei193PhosphoserineBy similarity1
Modified residuei202Phosphothreonine; by MAPK8, MAPK9 and MAPK10By similarity1
Modified residuei211PhosphoserineBy similarity1
Modified residuei308PhosphoserineBy similarity1
Modified residuei325PhosphoserineBy similarity1
Modified residuei327PhosphoserineBy similarity1
Modified residuei337PhosphoserineBy similarity1
Modified residuei352PhosphoserineBy similarity1
Modified residuei363PhosphoserineBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei404PhosphoserineBy similarity1
Modified residuei406PhosphoserineBy similarity1
Modified residuei408PhosphothreonineBy similarity1
Modified residuei441PhosphoserineBy similarity1
Modified residuei444PhosphoserineBy similarity1
Modified residuei445PhosphothreonineBy similarity1
Modified residuei466PhosphoserineBy similarity1
Modified residuei468PhosphoserineBy similarity1
Modified residuei469PhosphoserineBy similarity1
Modified residuei470PhosphoserineBy similarity1

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9R237.
PRIDEiQ9R237.

PTM databases

iPTMnetiQ9R237.
PhosphoSitePlusiQ9R237.

Expressioni

Tissue specificityi

Highly expressed in brain and pancreatic beta-cells. Weaker expression found in kidney.

Gene expression databases

BgeeiENSRNOG00000006938.

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). Interacts, via the PID domain, with ARHGEF28 (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 with DCLK2, VRK2 and MAP3K7 (By similarity).By similarity

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • JUN kinase binding Source: RGD
  • kinesin binding Source: UniProtKB
  • MAP-kinase scaffold activity Source: RGD
  • mitogen-activated protein kinase kinase binding Source: RGD
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ9R237. 6 interactors.
MINTiMINT-1500684.
STRINGi10116.ENSRNOP00000065176.

Structurei

Secondary structure

1708
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi490 – 492Combined sources3
Beta strandi511 – 517Combined sources7
Beta strandi521 – 527Combined sources7
Turni528 – 530Combined sources3
Beta strandi533 – 537Combined sources5
Helixi538 – 540Combined sources3
Beta strandi541 – 543Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FPDX-ray2.05A/B/C/D487-546[»]
2FPEX-ray1.75A/B/C/D/E/F/G/H487-546[»]
2FPFX-ray3.00A/B/C/D482-552[»]
ProteinModelPortaliQ9R237.
SMRiQ9R237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R237.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini485 – 546SH3PROSITE-ProRule annotationAdd BLAST62
Domaini558 – 697PIDPROSITE-ProRule annotationAdd BLAST140

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 282JNK-binding domain (JBD)Add BLAST157
Regioni154 – 173Minimal inhibitory domain (MID)Add BLAST20
Regioni280 – 468Interaction with MAP3K7By similarityAdd BLAST189
Regioni468 – 657Interaction with VRK2By similarityAdd BLAST190

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi350 – 357D-box 18
Motifi361 – 369D-box 29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 47Asp/Glu-rich (acidic)7
Compositional biasi107 – 115Asp/Glu-rich (acidic)9
Compositional biasi356 – 360Poly-Pro5

Domaini

The SH3 domain mediates homodimerization.

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

eggNOGiKOG3775. Eukaryota.
ENOG410ZFRJ. LUCA.
GeneTreeiENSGT00390000003908.
HOGENOMiHOG000231470.
HOVERGENiHBG018568.
InParanoidiQ9R237.
KOiK04434.
OMAiVQAEDYW.
PhylomeDBiQ9R237.
TreeFamiTF325073.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R237-1) [UniParc]FASTAAdd to basket
Also known as: JIP-1a, JIP-1b

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
MAERESGLSG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE
60 70 80 90 100
ITDECGISLQ CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA
110 120 130 140 150
SDTPGAEDDE EDDDELAAQR PGVGPSKAES GQEPASRSQG QGQGPGTGSG
160 170 180 190 200
DTYRPKRPTT LNLFPQVPRS QDTLNNNSLG KKHSWQDRVS RSSSPLKTGE
210 220 230 240 250
QTPPHEHICL SDELPPQGSP VPTQDRGTST DSPCRRTAAT QMAPPSGPPA
260 270 280 290 300
TAPGGRGHSH RDRIHYQADV RLEATEEIYL TPVQRPPDPA EPTSTFLPPT
310 320 330 340 350
ESRMSVSSDP DPAAYSVTAG RPHPSISEED EGFDCLSSPE QAEPPGGGWR
360 370 380 390 400
GSLGEPPPPP RASLSSDTSA LSYDSVKYTL VVDEHAQLEL VSLRPCFGDY
410 420 430 440 450
SDESDSATVY DNCASASSPY ESAIGEEYEE APQPRPPTCL SEDSTPDEPD
460 470 480 490 500
VHFSKKFLNV FMSGRSRSSS AESFGLFSCV INGEEHEQTH RAIFRFVPRH
510 520 530 540 550
EDELELEVDD PLLVELQAED YWYEAYNMRT GARGVFPAYY AIEVTKEPEH
560 570 580 590 600
MAALAKNSDW IDQFRVKFLG SVQVPYHKGN DVLCAAMQKI ATTRRLTVHF
610 620 630 640 650
NPPSSCVLEI SVRGVKIGVK ADEAQEAKGN KCSHFFQLKN ISFCGYHPKN
660 670 680 690 700
NKYFGFITKH PADHRFACHV FVSEDSTKAL AESVGRAFQQ FYKQFVEYTC

PTEDIYLE
Length:708
Mass (Da):77,318
Last modified:December 5, 2001 - v2
Checksum:i4923FD55F1C511F4
GO
Isoform 2 (identifier: Q9R237-2) [UniParc]FASTAAdd to basket
Also known as: JIP-1c, 2A

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

Show »
Length:699
Mass (Da):77,034
Checksum:i0DA066706C827D27
GO
Isoform 3 (identifier: Q9R237-3) [UniParc]FASTAAdd to basket
Also known as: JIP-1d

The sequence of this isoform differs from the canonical sequence as follows:
     69-93: Missing.
     708-708: E → EPMAQVQLQVDLEIKRAAAEQKLISEEDLNGAA

Show »
Length:715
Mass (Da):78,356
Checksum:i21DFC770F875277B
GO

Sequence cautioni

The sequence AAD22543 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAD38351 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38I → V in AAC62110 (Ref. 2) Curated1
Sequence conflicti149S → C in AAD22543 (PubMed:9442013).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0027671 – 33MAERE…PPNFR → MQLVLKMDSSPDNDSWLEDQ WERW in isoform 2. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_00276869 – 93Missing in isoform 3. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_002769708E → EPMAQVQLQVDLEIKRAAAE QKLISEEDLNGAA in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108959 mRNA. Translation: AAD22543.1. Different initiation.
AF092450 mRNA. Translation: AAC62110.1.
AF109772 mRNA. Translation: AAD38350.1.
AF109773 mRNA. Translation: AAD38351.1. Different initiation.
AF109774 mRNA. Translation: AAD38352.1.
RefSeqiNP_446229.1. NM_053777.1. [Q9R237-2]
UniGeneiRn.44266.

Genome annotation databases

EnsembliENSRNOT00000079746; ENSRNOP00000074684; ENSRNOG00000058478. [Q9R237-2]
GeneIDi116457.
KEGGirno:116457.
UCSCiRGD:70937. rat. [Q9R237-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108959 mRNA. Translation: AAD22543.1. Different initiation.
AF092450 mRNA. Translation: AAC62110.1.
AF109772 mRNA. Translation: AAD38350.1.
AF109773 mRNA. Translation: AAD38351.1. Different initiation.
AF109774 mRNA. Translation: AAD38352.1.
RefSeqiNP_446229.1. NM_053777.1. [Q9R237-2]
UniGeneiRn.44266.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FPDX-ray2.05A/B/C/D487-546[»]
2FPEX-ray1.75A/B/C/D/E/F/G/H487-546[»]
2FPFX-ray3.00A/B/C/D482-552[»]
ProteinModelPortaliQ9R237.
SMRiQ9R237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R237. 6 interactors.
MINTiMINT-1500684.
STRINGi10116.ENSRNOP00000065176.

PTM databases

iPTMnetiQ9R237.
PhosphoSitePlusiQ9R237.

Proteomic databases

PaxDbiQ9R237.
PRIDEiQ9R237.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000079746; ENSRNOP00000074684; ENSRNOG00000058478. [Q9R237-2]
GeneIDi116457.
KEGGirno:116457.
UCSCiRGD:70937. rat. [Q9R237-1]

Organism-specific databases

CTDi9479.
RGDi70937. Mapk8ip1.

Phylogenomic databases

eggNOGiKOG3775. Eukaryota.
ENOG410ZFRJ. LUCA.
GeneTreeiENSGT00390000003908.
HOGENOMiHOG000231470.
HOVERGENiHBG018568.
InParanoidiQ9R237.
KOiK04434.
OMAiVQAEDYW.
PhylomeDBiQ9R237.
TreeFamiTF325073.

Miscellaneous databases

EvolutionaryTraceiQ9R237.
PROiQ9R237.

Gene expression databases

BgeeiENSRNOG00000006938.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiJIP1_RAT
AccessioniPrimary (citable) accession number: Q9R237
Secondary accession number(s): O88979
, Q9R1H8, Q9WVI5, Q9WVI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: November 2, 2016
This is version 141 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.