JIP2_RAT
ID JIP2_RAT Reviewed; 835 AA.
AC G3V9M2; Q3B8P9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-835.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH SH3RF2.
RX PubMed=22128169; DOI=10.1074/jbc.m111.269431;
RA Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A., Gire S.,
RA Maes M.E., Xu Z., Greene L.A.;
RT "Sh3rf2/POSHER protein promotes cell survival by RING-mediated proteasomal
RT degradation of the c-Jun N-terminal kinase scaffold POSH (Plenty of SH3s)
RT protein.";
RL J. Biol. Chem. 287:2247-2256(2012).
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.
CC {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. Also binds the proline-
CC rich domain-containing splice variant of apolipoprotein E receptor 2
CC (ApoER2). Binds the TPR motif-containing C-terminal of kinesin light
CC chain. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin).
CC Interacts with DCLK2. Interacts with FGF13; enables the interaction
CC with MAPK13 and may regulate the MAPK8IP2 scaffolding activity.
CC Interacts with TIAM1 and TIAM2 (By similarity). Interacts with SH3RF2
CC (PubMed:22128169). {ECO:0000250|UniProtKB:Q13387,
CC ECO:0000250|UniProtKB:Q9ERE9, ECO:0000269|PubMed:22128169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13387}.
CC Note=Accumulates in cell surface projections.
CC {ECO:0000250|UniProtKB:Q13387}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
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DR EMBL; AC125982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474027; EDL76573.1; -; Genomic_DNA.
DR EMBL; BC105884; AAI05885.1; -; mRNA.
DR RefSeq; XP_001055248.1; XM_001055248.6.
DR RefSeq; XP_235565.5; XM_235565.9.
DR AlphaFoldDB; G3V9M2; -.
DR SMR; G3V9M2; -.
DR IntAct; G3V9M2; 1.
DR MINT; G3V9M2; -.
DR STRING; 10116.ENSRNOP00000052648; -.
DR PaxDb; G3V9M2; -.
DR ABCD; G3V9M2; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000055792; ENSRNOP00000052648; ENSRNOG00000032828.
DR GeneID; 315220; -.
DR CTD; 23542; -.
DR RGD; 1309727; Mapk8ip2.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000160461; -.
DR HOGENOM; CLU_006711_0_0_1; -.
DR InParanoid; G3V9M2; -.
DR OMA; HLAFACP; -.
DR OrthoDB; 372907at2759; -.
DR TreeFam; TF325073; -.
DR PRO; PR:G3V9M2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000032828; Expressed in frontal cortex and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0007254; P:JNK cascade; ISO:RGD.
DR GO; GO:0007617; P:mating behavior; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0046958; P:nonassociative learning; ISO:RGD.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:RGD.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISO:RGD.
DR GO; GO:0046328; P:regulation of JNK cascade; ISO:RGD.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:RGD.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISO:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
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..835
FT /note="C-Jun-amino-terminal kinase-interacting protein 2"
FT /id="PRO_0000444873"
FT DOMAIN 615..676
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 688..824
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..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..278
FT /note="JNK-binding domain (JBD)"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT REGION 242..509
FT /note="Necessary for interaction with FGF13"
FT /evidence="ECO:0000250|UniProtKB:Q13387"
FT REGION 369..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..579
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..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
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 379..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE9"
SQ SEQUENCE 835 AA; 90476 MW; D88871BA1FFB4398 CRC64;
MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL
SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE EDEEEEEEEE EEEDGDGDGR AGGGSGSQEL
SGESLIPSPS IEESHKLRPT TLHLTTLGAQ DSLNNNSNGG FTSAPPSSWQ ETVLRSPVQE
PLKELPAPLL PAEEEHHEVQ SLARPGCDCE GNQPPEPPAS GGASPSSDPG IEADLRSHSS
GGHEGRRSSQ ELSSPGSDSE EAGGARLGRM ISSISETELE LSSDSGSSSG RSSHLTNSIE
EASSPASEPE PEPEPEPLHE PPRRPAFLPV GQDDTNSEYE SGSESEPDLS EDADSPWLLS
NLVSRMISEG SSPIRCPGQC LSPPAPRPPE EAASQANPVP QDCPDPEAVA GPHVELVDMD
TLCGPPPPAP AAPRLGPAQS GPCLFLSNPT RDTITPLWAP PGRTARPGRS CSAACSEEEE
EDEEEDEEDE EDAEDSVIPP GSRTTGSTAP LDASLVYDAV KYTLVVDEHT QLELVSLRRC
AGLDNDSEED SSCEASEEEA GATLLGSDQV PEDASPDSPD LTFSKKFLNV FVNSTSRSSS
TESFGLFSCV VNGEEREQTH RAVFRFIPRH PDELELDVDD PVLVEAEEDD FWFRGFNMRT
GERGVFPAFY AHAVPGPAKD LLGSKRSPCW VDRFDVQFLG SVEVPCHQGN GILCAAMQKI
ATARKLTVHL RPPASCDLEI SLRGVKLSLS GGGPEFQRCS HFFQMKNISF CGCHPRNSCY
FGFITKHPLL SRFACHVFVS QESMRPVARS VGRAFLEYYQ EHLAFACPTE DIYLE
