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Q9ERE9 (JIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-Jun-amino-terminal kinase-interacting protein 2

Short name=JIP-2
Short name=JNK-interacting protein 2
Alternative name(s):
Islet-brain-2
Short name=IB-2
JNK MAP kinase scaffold protein 2
Mitogen-activated protein kinase 8-interacting protein 2
Gene names
Name:Mapk8ip2
Synonyms:Ib2, Jip2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length830 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Subunit structure

Forms homo-or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely JNK, MAPKK7 and MLK2, MLK3 and DLK By similarity. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Interacts with DCLK2. Ref.1 Ref.3

Subcellular location

Cytoplasm. Note: Accumulates in cell surface projections By similarity.

Tissue specificity

Highly expressed in brain. Expressed in all neurons. Also expressed in testis, primarily in the epididymal epidermis.

Induction

Upon neuron differentiation.

Sequence similarities

Belongs to the JIP scaffold family.

Contains 1 PID domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AK014339 differs from that shown. Reason: Erroneous termination at position 701. Translated as Cys.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainSH3 domain
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processJNK cascade

Inferred from direct assay Ref.1. Source: MGI

behavioral fear response

Inferred from mutant phenotype. Source: BHF-UCL

dendrite morphogenesis

Inferred from mutant phenotype. Source: BHF-UCL

mating behavior

Inferred from mutant phenotype. Source: BHF-UCL

nonassociative learning

Inferred from mutant phenotype. Source: BHF-UCL

regulation of JNK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype. Source: BHF-UCL

regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from mutant phenotype. Source: BHF-UCL

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype. Source: BHF-UCL

regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype. Source: BHF-UCL

social behavior

Inferred from mutant phenotype. Source: BHF-UCL

   Cellular componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from direct assay. Source: MGI

postsynaptic density

Inferred from direct assay. Source: BHF-UCL

   Molecular functionkinesin binding

Inferred from physical interaction. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ApplP145992EBI-74576,EBI-74135From a different organism.
Lrp1Q91ZX72EBI-74576,EBI-300955
Lrp2A2ARV42EBI-74576,EBI-300875

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 830830C-Jun-amino-terminal kinase-interacting protein 2
PRO_0000220632

Regions

Domain610 – 67162SH3
Domain683 – 819137PID
Region111 – 278168JNK-binding domain (JBD)
Compositional bias30 – 367Asp/Glu-rich (acidic)
Compositional bias85 – 10420Asp/Glu-rich (acidic)
Compositional bias154 – 1574Poly-Asn
Compositional bias282 – 29312Ser-rich
Compositional bias420 – 43718Pro-rich
Compositional bias472 – 48716Asp/Glu-rich (acidic)

Experimental info

Sequence conflict2161P → Q in AK014339. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ERE9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7EC8EAD19A90163C

FASTA83089,900
        10         20         30         40         50         60 
MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL 

        70         80         90        100        110        120 
SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEEEEEEEE EEEDGDRQGK AGGGPGSQAL 

       130        140        150        160        170        180 
AGDSLIPSPS LEESHKLRPT TLHLTTLGAQ DSLNNNNGGF TSAPPSSWQE TVLRSPAQEP 

       190        200        210        220        230        240 
LKELPAPLLP AEEERHEVQS LARPGCDCEG NQPPEPPASS GGASPSSDPG IEADLRSHSS 

       250        260        270        280        290        300 
GGHEGRRSSQ ELSSPGSDSE DAGGARLGRM ISSISETELE LSSDGGSSSG RSSHLTNSIE 

       310        320        330        340        350        360 
EASSPASEPE PEPEPLHEPP RRPAFLPVGQ DDTNSEYESG SESEPDLSED ADSPWLLSNL 

       370        380        390        400        410        420 
VSRMISEGSS PIRCPGQCLS PAPRLPEEAA SQANSVPQDC QDPEAGPHVE LVDMDTLCGP 

       430        440        450        460        470        480 
PPPAPAAPRL GPAQPGPCLF LSNPTRDTIT PLWATPGRTA RPGRSCSAAC SEEEEEDEEE 

       490        500        510        520        530        540 
DEEDEEDAED SVVPPGSRTT GSTAPLDASL VYDAVKYTLV VDEHTQLELV SLRRCAGLGN 

       550        560        570        580        590        600 
DSEEDSSCEA SEEEAGATLL GSDQVPEDAS PDSPDLTFSK KFLNVFVNST SRSSSTESFG 

       610        620        630        640        650        660 
LFSCVVNGEE REQTHRAVFR FIPRHPDELE LDVDDPVLVE AEEDDFWFRG FNMRTGERGV 

       670        680        690        700        710        720 
FPAFYAHAVP GPAKDLLGSK RSPCWVDRFD VQFLGSVEVP CHQGNGILCA AMQKIATARK 

       730        740        750        760        770        780 
LTVHLRPPAS CDLEISLRGV KLSLSGGGPE FQRCSHFFQM KNISFCGCHP RNSCYFGFIT 

       790        800        810        820        830 
KHPLLSRFAC HVFVSQESMR PVARSVGRAF LEYYQEHLAF ACPTEDIYLE 

« Hide

References

« Hide 'large scale' references
[1]"The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2."
Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M., Herz J., Schneider W.J., Nimpf J.
J. Biol. Chem. 275:25625-25632(2000) [PubMed: 10827199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APOER2.
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic head.
[3]"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: 16628014] [Abstract]
Cited for: INTERACTION WITH DCLK2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF310135 mRNA. Translation: AAG31800.1.
AK014339 mRNA. No translation available.
IPIIPI00112307.
RefSeqNP_068740.3. NM_021921.3.
UniGeneMm.173337.
Mm.482169.

3D structure databases

ProteinModelPortalQ9ERE9.
SMRQ9ERE9. Positions 612-666, 687-820.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9ERE9. 5 interactions.
STRINGQ9ERE9.

PTM databases

PhosphoSiteQ9ERE9.

Proteomic databases

PRIDEQ9ERE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023291; ENSMUSP00000023291; ENSMUSG00000022619.
GeneID60597.
KEGGmmu:60597.

Organism-specific databases

CTD23542.
MGIMGI:1926555. Mapk8ip2.

Phylogenomic databases

GeneTreeENSGT00390000003908.
HOGENOMHBG713638.
HOVERGENHBG018568.
InParanoidQ9ERE9.
OMASDPGIEA.
OrthoDBEOG4Q84X6.
PhylomeDBQ9ERE9.

Gene expression databases

ArrayExpressQ9ERE9.
BgeeQ9ERE9.
GenevestigatorQ9ERE9.
GermOnlineENSMUSG00000022619. Mus musculus.

Family and domain databases

InterProIPR011993. PH_type.
IPR006020. PTyr_interaction_dom.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
KOK04435.
PfamPF00640. PID. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameJIP2_MOUSE
AccessionPrimary (citable) accession number: Q9ERE9
Secondary accession number(s): Q9CXI4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families