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C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2)

 JIP2_MOUSE              Reviewed;         830 AA.
Q9ERE9; Q9CXI4;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 144.
RecName: Full=C-Jun-amino-terminal kinase-interacting protein 2;
Short=JIP-2;
Short=JNK-interacting protein 2;
AltName: Full=Islet-brain-2;
Short=IB-2;
AltName: Full=JNK MAP kinase scaffold protein 2;
AltName: Full=Mitogen-activated protein kinase 8-interacting protein 2;
Name=Mapk8ip2; Synonyms=Ib2, Jip2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH APOER2.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10827199; DOI=10.1074/jbc.M004119200;
Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M.,
Herz J., Schneider W.J., Nimpf J.;
"The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and
-2.";
J. Biol. Chem. 275:25625-25632(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic head;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
INTERACTION WITH FGF13 AND MAPK13.
PubMed=11378392; DOI=10.1016/S0960-9822(01)00232-9;
Schoorlemmer J., Goldfarb M.;
"Fibroblast growth factor homologous factors are intracellular
signaling proteins.";
Curr. Biol. 11:793-797(2001).
[4]
INTERACTION WITH DCLK2.
PubMed=16628014; DOI=10.4161/cc.5.9.2715;
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.;
"Common and divergent roles for members of the mouse DCX
superfamily.";
Cell Cycle 5:976-983(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-304 AND
SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
INTERACTION WITH TIAM1 AND TIAM2.
PubMed=19893486; DOI=10.1038/emboj.2009.323;
Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N.,
Watanabe T., Kaibuchi K., Hakoshima T.;
"The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
module.";
EMBO J. 29:236-250(2010).
-!- 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). {ECO:0000250}.
-!- SUBUNIT: Forms homo-or heterooligomeric complexes. Binds specific
components of the JNK signaling pathway namely JNK1, JNK2, JNK3,
MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13 (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. Interacts with FGF13; enables the interaction with MAPK13
and may regulate the MAPK8IP2 scaffolding activity. Interacts with
TIAM1 and TIAM2 (PubMed:10827199, PubMed:11378392,
PubMed:16628014, PubMed:19893486). Interacts with SH3RF2 (By
similarity). {ECO:0000250|UniProtKB:G3V9M2,
ECO:0000250|UniProtKB:Q13387, ECO:0000269|PubMed:10827199,
ECO:0000269|PubMed:11378392, ECO:0000269|PubMed:16628014,
ECO:0000269|PubMed:19893486}.
-!- INTERACTION:
P14599:Appl (xeno); NbExp=2; IntAct=EBI-74576, EBI-74135;
Q91ZX7:Lrp1; NbExp=2; IntAct=EBI-74576, EBI-300955;
A2ARV4:Lrp2; NbExp=2; IntAct=EBI-74576, EBI-300875;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}.
Note=Accumulates in cell surface projections.
{ECO:0000250|UniProtKB:Q13387}.
-!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in all
neurons. Also expressed in testis, primarily in the epididymal
epidermis.
-!- INDUCTION: Upon neuron differentiation.
-!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK014339; Type=Erroneous termination; Positions=701; Note=Translated as Cys.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF310135; AAG31800.1; -; mRNA.
EMBL; AK014339; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS27752.1; -.
RefSeq; NP_068740.3; NM_021921.3.
UniGene; Mm.173337; -.
UniGene; Mm.482169; -.
ProteinModelPortal; Q9ERE9; -.
SMR; Q9ERE9; -.
BioGrid; 208626; 4.
IntAct; Q9ERE9; 8.
MINT; Q9ERE9; -.
STRING; 10090.ENSMUSP00000023291; -.
iPTMnet; Q9ERE9; -.
PhosphoSitePlus; Q9ERE9; -.
MaxQB; Q9ERE9; -.
PaxDb; Q9ERE9; -.
PRIDE; Q9ERE9; -.
Ensembl; ENSMUST00000023291; ENSMUSP00000023291; ENSMUSG00000022619.
GeneID; 60597; -.
KEGG; mmu:60597; -.
UCSC; uc007xgx.2; mouse.
CTD; 23542; -.
MGI; MGI:1926555; Mapk8ip2.
eggNOG; KOG3775; Eukaryota.
eggNOG; ENOG410ZFRJ; LUCA.
GeneTree; ENSGT00390000003908; -.
HOGENOM; HOG000231470; -.
HOVERGEN; HBG018568; -.
InParanoid; Q9ERE9; -.
KO; K04435; -.
OMA; HKHRPTT; -.
OrthoDB; EOG091G0T9G; -.
PhylomeDB; Q9ERE9; -.
TreeFam; TF325073; -.
PRO; PR:Q9ERE9; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022619; Expressed in 202 organ(s), highest expression level in supraoptic nucleus.
ExpressionAtlas; Q9ERE9; baseline and differential.
Genevisible; Q9ERE9; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:MGI.
GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:BHF-UCL.
GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:BHF-UCL.
GO; GO:0007254; P:JNK cascade; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0007617; P:mating behavior; IMP:BHF-UCL.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI.
GO; GO:0046958; P:nonassociative learning; IMP:BHF-UCL.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:BHF-UCL.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL.
GO; GO:0010469; P:regulation of signaling receptor activity; IMP:BHF-UCL.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
CDD; cd11942; SH3_JIP2; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035637; JIP2_SH3.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF00640; PID; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00462; PTB; 1.
SMART; SM00326; SH3; 1.
PROSITE; PS01179; PID; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
SH3 domain.
CHAIN 1 830 C-Jun-amino-terminal kinase-interacting
protein 2.
/FTId=PRO_0000220632.
DOMAIN 610 671 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 683 819 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 111 278 JNK-binding domain (JBD).
REGION 242 504 Necessary for interaction with FGF13.
{ECO:0000250|UniProtKB:Q13387}.
COMPBIAS 30 36 Asp/Glu-rich (acidic).
COMPBIAS 85 104 Asp/Glu-rich (acidic).
COMPBIAS 154 157 Poly-Asn.
COMPBIAS 282 293 Ser-rich.
COMPBIAS 420 437 Pro-rich.
COMPBIAS 472 487 Asp/Glu-rich (acidic).
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 216 216 P -> Q (in Ref. 2; AK014339).
{ECO:0000305}.
SEQUENCE 830 AA; 89900 MW; 7EC8EAD19A90163C CRC64;
MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL
SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEEEEEEEE EEEDGDRQGK AGGGPGSQAL
AGDSLIPSPS LEESHKLRPT TLHLTTLGAQ DSLNNNNGGF TSAPPSSWQE TVLRSPAQEP
LKELPAPLLP AEEERHEVQS LARPGCDCEG NQPPEPPASS GGASPSSDPG IEADLRSHSS
GGHEGRRSSQ ELSSPGSDSE DAGGARLGRM ISSISETELE LSSDGGSSSG RSSHLTNSIE
EASSPASEPE PEPEPLHEPP RRPAFLPVGQ DDTNSEYESG SESEPDLSED ADSPWLLSNL
VSRMISEGSS PIRCPGQCLS PAPRLPEEAA SQANSVPQDC QDPEAGPHVE LVDMDTLCGP
PPPAPAAPRL GPAQPGPCLF LSNPTRDTIT PLWATPGRTA RPGRSCSAAC SEEEEEDEEE
DEEDEEDAED SVVPPGSRTT GSTAPLDASL VYDAVKYTLV VDEHTQLELV SLRRCAGLGN
DSEEDSSCEA SEEEAGATLL GSDQVPEDAS PDSPDLTFSK KFLNVFVNST SRSSSTESFG
LFSCVVNGEE REQTHRAVFR FIPRHPDELE LDVDDPVLVE AEEDDFWFRG FNMRTGERGV
FPAFYAHAVP GPAKDLLGSK RSPCWVDRFD VQFLGSVEVP CHQGNGILCA AMQKIATARK
LTVHLRPPAS CDLEISLRGV KLSLSGGGPE FQRCSHFFQM KNISFCGCHP RNSCYFGFIT
KHPLLSRFAC HVFVSQESMR PVARSVGRAF LEYYQEHLAF ACPTEDIYLE


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