JIP2_MOUSE
ID JIP2_MOUSE Reviewed; 830 AA.
AC Q9ERE9; Q9CXI4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 2;
DE Short=JIP-2;
DE Short=JNK-interacting protein 2;
DE AltName: Full=Islet-brain-2;
DE Short=IB-2;
DE AltName: Full=JNK MAP kinase scaffold protein 2;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 2;
GN Name=Mapk8ip2; Synonyms=Ib2, Jip2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH APOER2.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10827199; DOI=10.1074/jbc.m004119200;
RA Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M., Herz J.,
RA Schneider W.J., Nimpf J.;
RT "The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2.";
RL J. Biol. Chem. 275:25625-25632(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH FGF13 AND MAPK13.
RX PubMed=11378392; DOI=10.1016/s0960-9822(01)00232-9;
RA Schoorlemmer J., Goldfarb M.;
RT "Fibroblast growth factor homologous factors are intracellular signaling
RT proteins.";
RL Curr. Biol. 11:793-797(2001).
RN [4]
RP INTERACTION WITH DCLK2.
RX PubMed=16628014; DOI=10.4161/cc.5.9.2715;
RA Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
RA Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
RT "Common and divergent roles for members of the mouse DCX superfamily.";
RL Cell Cycle 5:976-983(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-304 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH TIAM1 AND TIAM2.
RX PubMed=19893486; DOI=10.1038/emboj.2009.323;
RA Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T.,
RA Kaibuchi K., Hakoshima T.;
RT "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
RT module.";
RL EMBO J. 29:236-250(2010).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module. JIP2
CC inhibits IL1 beta-induced apoptosis in insulin-secreting cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific
CC components of the JNK signaling pathway namely JNK1, JNK2, JNK3,
CC MAP2K7, MAP3K10, MAP3K11, MAP3K12 and MAPK13 (By similarity). Also
CC binds the proline-rich domain-containing splice variant of
CC apolipoprotein E receptor 2 (ApoER2). Binds the TPR motif-containing C-
CC terminal of kinesin light chain. Binds the cytoplasmic tails of LRP1
CC and LRP2 (Megalin). Interacts with DCLK2. Interacts with FGF13; enables
CC the interaction with MAPK13 and may regulate the MAPK8IP2 scaffolding
CC activity. Interacts with TIAM1 and TIAM2 (PubMed:10827199,
CC PubMed:11378392, PubMed:16628014, PubMed:19893486). Interacts with
CC SH3RF2 (By similarity). {ECO:0000250|UniProtKB:G3V9M2,
CC ECO:0000250|UniProtKB:Q13387, ECO:0000269|PubMed:10827199,
CC ECO:0000269|PubMed:11378392, ECO:0000269|PubMed:16628014,
CC ECO:0000269|PubMed:19893486}.
CC -!- INTERACTION:
CC Q9ERE9; Q91ZX7: Lrp1; NbExp=2; IntAct=EBI-74576, EBI-300955;
CC Q9ERE9; A2ARV4: Lrp2; NbExp=2; IntAct=EBI-74576, EBI-300875;
CC Q9ERE9; P14599: Appl; Xeno; NbExp=2; IntAct=EBI-74576, EBI-74135;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}.
CC Note=Accumulates in cell surface projections.
CC {ECO:0000250|UniProtKB:Q13387}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in all
CC neurons. Also expressed in testis, primarily in the epididymal
CC epidermis.
CC -!- INDUCTION: Upon neuron differentiation.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK014339; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF310135; AAG31800.1; -; mRNA.
DR EMBL; AK014339; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS27752.1; -.
DR RefSeq; NP_068740.3; NM_021921.3.
DR AlphaFoldDB; Q9ERE9; -.
DR SMR; Q9ERE9; -.
DR BioGRID; 208626; 5.
DR IntAct; Q9ERE9; 8.
DR MINT; Q9ERE9; -.
DR STRING; 10090.ENSMUSP00000023291; -.
DR iPTMnet; Q9ERE9; -.
DR PhosphoSitePlus; Q9ERE9; -.
DR MaxQB; Q9ERE9; -.
DR PaxDb; Q9ERE9; -.
DR PRIDE; Q9ERE9; -.
DR ProteomicsDB; 269235; -.
DR ABCD; Q9ERE9; 1 sequenced antibody.
DR Antibodypedia; 28835; 254 antibodies from 28 providers.
DR DNASU; 60597; -.
DR Ensembl; ENSMUST00000023291; ENSMUSP00000023291; ENSMUSG00000022619.
DR GeneID; 60597; -.
DR KEGG; mmu:60597; -.
DR UCSC; uc007xgx.2; mouse.
DR CTD; 23542; -.
DR MGI; MGI:1926555; Mapk8ip2.
DR VEuPathDB; HostDB:ENSMUSG00000022619; -.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000160461; -.
DR HOGENOM; CLU_006711_0_0_1; -.
DR InParanoid; Q9ERE9; -.
DR OMA; HLAFACP; -.
DR OrthoDB; 372907at2759; -.
DR PhylomeDB; Q9ERE9; -.
DR TreeFam; TF325073; -.
DR BioGRID-ORCS; 60597; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Mapk8ip2; mouse.
DR PRO; PR:Q9ERE9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9ERE9; protein.
DR Bgee; ENSMUSG00000022619; Expressed in supraoptic nucleus and 165 other tissues.
DR ExpressionAtlas; Q9ERE9; baseline and differential.
DR Genevisible; Q9ERE9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:BHF-UCL.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0007617; P:mating behavior; IMP:BHF-UCL.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0046958; P:nonassociative learning; IMP:BHF-UCL.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:BHF-UCL.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IMP:BHF-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR CDD; cd11942; SH3_JIP2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035637; JIP2_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..830
FT /note="C-Jun-amino-terminal kinase-interacting protein 2"
FT /id="PRO_0000220632"
FT DOMAIN 610..671
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 683..819
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..278
FT /note="JNK-binding domain (JBD)"
FT REGION 242..504
FT /note="Necessary for interaction with FGF13"
FT /evidence="ECO:0000250|UniProtKB:Q13387"
FT REGION 367..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 216
FT /note="P -> Q (in Ref. 2; AK014339)"
FT /evidence="ECO:0000305"
SQ 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
