ID   E9Q6B6_MOUSE            Unreviewed;      1300 AA.
AC   E9Q6B6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Mitogen-activated protein kinase 8 interacting protein 3 {ECO:0000313|Ensembl:ENSMUSP00000113753.2};
GN   Name=Mapk8ip3 {ECO:0000313|Ensembl:ENSMUSP00000113753.2,
GN   ECO:0000313|MGI:MGI:1353598};
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 {ECO:0000313|Ensembl:ENSMUSP00000113753.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000113753.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113753.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [4] {ECO:0000313|Ensembl:ENSMUSP00000113753.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113753.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC       {ECO:0000256|ARBA:ARBA00009866}.
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DR   RefSeq; NP_001156925.1; NM_001163453.1.
DR   SMR; E9Q6B6; -.
DR   MaxQB; E9Q6B6; -.
DR   PeptideAtlas; E9Q6B6; -.
DR   ProteomicsDB; 314721; -.
DR   Antibodypedia; 3958; 188 antibodies from 34 providers.
DR   DNASU; 30957; -.
DR   Ensembl; ENSMUST00000121787.8; ENSMUSP00000113753.2; ENSMUSG00000024163.18.
DR   GeneID; 30957; -.
DR   UCSC; uc012amv.1; mouse.
DR   AGR; MGI:1353598; -.
DR   CTD; 23162; -.
DR   MGI; MGI:1353598; Mapk8ip3.
DR   VEuPathDB; HostDB:ENSMUSG00000024163; -.
DR   GeneTree; ENSGT00940000153496; -.
DR   HOGENOM; CLU_003841_0_0_1; -.
DR   OrthoDB; 3685563at2759; -.
DR   BioGRID-ORCS; 30957; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Mapk8ip3; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000024163; Expressed in dentate gyrus of hippocampal formation granule cell and 258 other cell types or tissues.
DR   ExpressionAtlas; E9Q6B6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:InterPro.
DR   Gene3D; 1.20.58.1770; -; 1.
DR   Gene3D; 1.20.5.1000; arf6 gtpase in complex with a specific effector, jip4; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR039911; JIP3/JIP4.
DR   InterPro; IPR032486; JIP_LZII.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR034743; RH1.
DR   InterPro; IPR034744; RH2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13886:SF3; C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 3; 1.
DR   PANTHER; PTHR13886; JNK/SAPK-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF16471; JIP_LZII; 1.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   Pfam; PF19056; WD40_2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51776; RH1; 1.
DR   PROSITE; PS51777; RH2; 1.
DR   Genevisible; E9Q6B6; MM.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Proteomics identification {ECO:0007829|EPD:E9Q6B6,
KW   ECO:0007829|MaxQB:E9Q6B6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          12..100
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          484..558
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          183..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          412..460
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        223..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1300 AA;  143445 MW;  1257BE83224175B6 CRC64;
     MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
     NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
     ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
     RSKMQQVGGS GQTESSLPGR SRKERPTSLN VFPLADGMCP NDEMSESGQS SAAATPSTTG
     TKSNTPTSSV PSAAVTPLNE SLQPLGDYVS VTKNNKQARE KRNSRNMEVQ VTQEMRNVSI
     GMGSSDEWSD VQDIIDSTPE LDVCPETRLE RTGSSPTQGI VNKAFGINTD SLYHELSTAG
     SEVIGDVDEG ADLLGEFSGM GKEVGNLLLE NSQLLETKNA LNVVKNDLIA KVDQLSGEQE
     VLKGELEAAK QAKVKLENRI KELEEELKRV KSEAVTARRE PREEVEDVSS YLCTELDKIP
     MAQRRRFTRV EMARVLMERN QYKERLMELQ EAVRWTEMIR ASREHPSVQE KKKSTIWQFF
     SRLFSSSSSP PPAKRSYPSV NIHYKSPTAA GFSQRRSHAL CQISAGSRPL EFFPDDDCTS
     SARREQKREQ YRQVREHVRN DDGRLQACGW SLPAKYKQLS PNGGQEDTRM KNVPVPVYCR
     PLVEKDPSTK LWCAAGVNLS GWKPHEEDSS NGPKPVPGRD PLTCDREGEG EPKSTHPSPE
     KKKAKETPEA DATSSRVWIL TSTLTTSKVV IIDANQPGTI VDQFTVCNAH VLCISSIPAA
     SDSDYPPGEM FLDSDVNPED SGADGVLAGI TLVGCATRCN VPRSNCSSRG DTPVLDKGQG
     DVATTANGKV NPSQSTEEAT EATEVPDPGP SESEATTVRP GPLTEHVFTD PAPTPSSSTQ
     PASENGSESN GTIVQPQVEP SGELSTTTSS AAPTMWLGAQ NGWLYVHSAV ANWKKCLHSI
     KLKDSVLSLV HVKGRVLVAL ADGTLAIFHR GEDGQWDLSN YHLMDLGHPH HSIRCMAVVN
     DRVWCGYKNK VHVIQPKTMQ IEKSFDAHPR RESQVRQLAW IGDGVWVSIR LDSTLRLYHA
     HTHQHLQDVD IEPYVSKMLG TGKLGFSFVR ITALLIAGNR LWVGTGNGVV ISIPLTETVV
     LHRGQLLGLR ANKTSPTSGE GTRPGGIIHV YGDDSSDKAA SSFIPYCSMA QAQLCFHGHR
     DAVKFFVSVP GNVLATLNGS VLDSPSEGPG PAAPAADAEG QKLKNALVLS GGEGYIDFRI
     GDGEDDETEE CAGDVNQTKP SLSKAERSHI IVWQVSYTPE
//