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Q13387 (JIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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, PRKM8IPL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. May function as a regulator of vesicle transport, through interations with the JNK-signaling components and motor proteins 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. 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 By similarity.

Subcellular location

Cytoplasm. Note: Accumulates in cell surface projections.

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.

Sequence similarities

Belongs to the JIP scaffold family.

Contains 1 PID domain.

Contains 1 SH3 domain.

Sequence caution

The sequence CAA16714.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processMAPKKK cascade

Inferred from direct assay. Source: MGI

behavioral fear response

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

nonassociative learning

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of anti-apoptosis

Non-traceable author statement Ref.2. Source: UniProtKB

regulation of JNK cascade

Inferred from direct assay Ref.1. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: BHF-UCL

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

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: BHF-UCL

signal complex assembly

Traceable author statement. Source: ProtInc

social behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

postsynaptic density

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular functionMAP-kinase scaffold activity

Non-traceable author statement Ref.1. Source: UniProtKB

beta-amyloid binding

Non-traceable author statement. Source: UniProtKB

kinesin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase activator activity

Inferred from direct assay. Source: MGI

protein kinase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: 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.
Isoform 2 (identifier: Q13387-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MADRAEMFSL...LSYDSDHCEK → MLPDFPSPSTWAPGLLLPSGPALLSPSVLQ
Isoform 3 (identifier: Q13387-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MADRAEMFSL...LSYDSDHCEK → MLPDFPSPSTWAPGLLLPSGPALLSPSVLQ
     152-394: Missing.
     415-439: Missing.
     768-768: C → CEAPQGAAFQWERGVDRKRVLQTRGNVQPHLGAGQGAALNRATEGSSTGSEKGEWTPLVIMELTQSVNSC
Note: Might be artifactual as it is only predicted from a genomic sequence.
Isoform 4 (identifier: Q13387-4)

The sequence of this isoform differs from the canonical sequence as follows:
     88-468: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 824824C-Jun-amino-terminal kinase-interacting protein 2
PRO_0000220631

Regions

Domain604 – 66562SH3
Domain677 – 813137PID
Region110 – 275166JNK-binding domain (JBD)
Compositional bias30 – 367Asp/Glu-rich (acidic)
Compositional bias85 – 10319Asp/Glu-rich (acidic)
Compositional bias279 – 29113Ser-rich
Compositional bias417 – 43418Pro-rich
Compositional bias469 – 48113Asp/Glu-rich (acidic)

Natural variations

Alternative sequence1 – 5757MADRA…DHCEK → MLPDFPSPSTWAPGLLLPSG PALLSPSVLQ in isoform 2 and isoform 3.
VSP_002770
Alternative sequence88 – 468381Missing in isoform 4.
VSP_002771
Alternative sequence152 – 394243Missing in isoform 3.
VSP_002772
Alternative sequence415 – 43925Missing in isoform 3.
VSP_002773
Alternative sequence7681C → CEAPQGAAFQWERGVDRKRV LQTRGNVQPHLGAGQGAALN RATEGSSTGSEKGEWTPLVI MELTQSVNSC in isoform 3.
VSP_002774
Natural variant7431P → L.
Corresponds to variant rs1140555 [ dbSNP | Ensembl ].
VAR_049666

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 7EFC8F3BC58E37BB

FASTA82487,975
        10         20         30         40         50         60 
MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL 

        70         80         90        100        110        120 
SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEDEEEEEE EEEGDGEGQE GGDPGSEAPA 

       130        140        150        160        170        180 
PGPLIPSPSV EEPHKHRPTT LRLTTLGAQD SLNNNGGFDL VRPASWQETA LCSPAPEALR 

       190        200        210        220        230        240 
ELPGPLPATD TGPGGAQSPV RPGCDCEGNR PAEPPAPGGT SPSSDPGIEA DLRSRSSGGR 

       250        260        270        280        290        300 
GGRRSSQELS SPGSDSEDAG GARLGRMISS ISETELELSS DGGSSSSGRS SHLTNSIEEA 

       310        320        330        340        350        360 
SSPASEPEPP REPPRRPAFL PVGPDDTNSE YESGSESEPD LSEDADSPWL LSNLVSRMIS 

       370        380        390        400        410        420 
EGSSPIRCPG QCLSPAPRPP GEPVSPAGGA AQDSQDPEAA AGPGGVELVD METLCAPPPP 

       430        440        450        460        470        480 
APAAPRPGPA QPGPCLFLSN PTRDTITPLW AAPGRAARPG RACSAACSEE EDEEDDEEEE 

       490        500        510        520        530        540 
DAEDSAGSPG GRGTGPSAPR DASLVYDAVK YTLVVDEHTQ LELVSLRRCA GLGHDSEEDS 

       550        560        570        580        590        600 
GGEASEEEAG AALLGGGQVS GDTSPDSPDL TFSKKFLNVF VNSTSRSSST ESFGLFSCLV 

       610        620        630        640        650        660 
NGEEREQTHR AVFRFIPRHP DELELDVDDP VLVEAEEDDF WFRGFNMRTG ERGVFPAFYA 

       670        680        690        700        710        720 
HAVPGPAKDL LGSKRSPCWV ERFDVQFLGS VEVPCHQGNG ILCAAMQKIA TARKLTVHLR 

       730        740        750        760        770        780 
PPASCDLEIS LRGVKLSLSG GGPEFQRCSH FFQMKNISFC GCHPRNSCYF GFITKHPLLS 

       790        800        810        820 
RFACHVFVSQ ESMRPVAQSV GRAFLEYYQE HLAYACPTED IYLE 

« Hide

Isoform 2 [UniParc].

Checksum: 715D63743DF04E7B
Show »

FASTA79784,711
Isoform 3 [UniParc].

Checksum: 863EA918E833DCAE
Show »

FASTA59864,934
Isoform 4 [UniParc].

Checksum: 6340E55966B6EFC3
Show »

FASTA44349,070

References

« Hide 'large scale' references
[1]"The JIP group of mitogen-activated protein kinase scaffold proteins."
Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.
Mol. Cell. Biol. 19:7245-7254(1999) [PubMed: 10490659] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"cDNA cloning and mapping of a novel islet-brain/JNK interacting protein."
Negri S., Oberson A., Steinmann M., Sauser C., Nicod P., Waeber G., Schorderet D.F., Bonny C.
Genomics 64:324-330(2000) [PubMed: 10756100] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain and Insulinoma.
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Adams M.D.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[6]"Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
Genome Res. 13:27-36(2003) [PubMed: 12529303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-824.
[7]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 599-824 (ISOFORM 1).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF136382 mRNA. Translation: AAF00980.1.
AF218778 mRNA. Translation: AAF32323.1.
U62317 Genomic DNA. Translation: AAB03340.1.
BC009940 mRNA. Translation: AAH09940.2.
AL021708 mRNA. Translation: CAA16714.1. Different initiation.
U79261 mRNA. Translation: AAB50207.1.
IPIIPI00031777.
IPI00221227.
IPI00221228.
IPI00221229.
RefSeqNP_036456.1. NM_012324.3.
NP_057515.1. NM_016431.3.
UniGeneHs.558180.

3D structure databases

ProteinModelPortalQ13387.
SMRQ13387. Positions 606-814.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13387. 1 interaction.
MINTMINT-111751.
STRINGQ13387.

PTM databases

PhosphoSiteQ13387.

Polymorphism databases

DMDM17433017.

Proteomic databases

PRIDEQ13387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329492; ENSP00000330572; ENSG00000008735.
GeneID23542.
KEGGhsa:23542.

Organism-specific databases

CTD23542.
GeneCardsGC22P051039.
H-InvDBHIX0027837.
HGNCHGNC:6883. MAPK8IP2.
HPAHPA034780.
MIM607755. gene.
neXtProtNX_Q13387.
PharmGKBPA30627.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11185.
HOGENOMHBG713638.
HOVERGENHBG018568.
InParanoidQ13387.

Gene expression databases

ArrayExpressQ13387.
BgeeQ13387.
CleanExHS_MAPK8IP2.
GenevestigatorQ13387.
GermOnlineENSG00000008735. Homo sapiens.

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

NextBio46052.
SOURCESearch...

Entry information

Entry nameJIP2_HUMAN
AccessionPrimary (citable) accession number: Q13387
Secondary accession number(s): Q96G62 expand/collapse secondary AC list , Q99771, Q9NZ59, Q9UKQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: January 25, 2012
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families