MABP1_MOUSE
ID MABP1_MOUSE Reviewed; 1503 AA.
AC Q6NS57; A2AWL8; Q80TW5; Q9R0L0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Mitogen-activated protein kinase-binding protein 1;
DE AltName: Full=JNK-binding protein 1;
DE Short=JNKBP-1;
GN Name=Mapkbp1; Synonyms=Jnkbp1, Kiaa0596;
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] (ISOFORM 2), FUNCTION, INTERACTION WITH MAPK10,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10471813; DOI=10.1016/s0014-5793(99)01084-4;
RA Koyano S., Ito M., Takamatsu N., Shiba T., Yamamoto K., Yoshioka K.;
RT "A novel Jun N-terminal kinase (JNK)-binding protein that enhances the
RT activation of JNK by MEK kinase 1 and TGF-beta-activated kinase 1.";
RL FEBS Lett. 457:385-388(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 441-1503.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Negative regulator of NOD2 function. It down-regulates NOD2-
CC induced processes such as activation of NF-kappa-B signaling, IL8
CC secretion and antibacterial response (By similarity). Involved in JNK
CC signaling pathway (PubMed:10471813). {ECO:0000250|UniProtKB:O60336,
CC ECO:0000269|PubMed:10471813}.
CC -!- SUBUNIT: Can form homodimers (via C-terminus). Interacts (via C-
CC terminus) with WDR62 (via C-terminus). Interacts with MAPK9. Interacts
CC (via N-terminus) with NOD2; the interaction is enhanced in presence of
CC muramyl dipeptide (MDP) (By similarity). Interacts with MAPK10
CC (PubMed:10471813). {ECO:0000250|UniProtKB:O60336,
CC ECO:0000269|PubMed:10471813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60336}. Nucleus
CC {ECO:0000250|UniProtKB:O60336}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:O60336}. Note=Not detected in the cilium.
CC Localized around the poles of the mitotic spindle from prophase to
CC anaphase in mitotic cells. {ECO:0000250|UniProtKB:O60336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NS57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NS57-2; Sequence=VSP_033636;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression observed
CC in brain. {ECO:0000269|PubMed:10471813}.
CC -!- DOMAIN: The N-terminal WD40 domain is necessary for the interaction
CC with NOD2 and down-regulation of NOD2 function.
CC {ECO:0000250|UniProtKB:O60336}.
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DR EMBL; AB029482; BAA85449.1; -; mRNA.
DR EMBL; AL954662; CAM21732.1; -; Genomic_DNA.
DR EMBL; AL833774; CAM21732.1; JOINED; Genomic_DNA.
DR EMBL; AL833774; CAM22679.1; -; Genomic_DNA.
DR EMBL; AL954662; CAM22679.1; JOINED; Genomic_DNA.
DR EMBL; BC070449; AAH70449.1; -; mRNA.
DR EMBL; AK122323; BAC65605.3; -; Transcribed_RNA.
DR CCDS; CCDS16612.1; -. [Q6NS57-1]
DR CCDS; CCDS89541.1; -. [Q6NS57-2]
DR RefSeq; NP_036071.3; NM_011941.3.
DR AlphaFoldDB; Q6NS57; -.
DR SMR; Q6NS57; -.
DR BioGRID; 204947; 8.
DR ELM; Q6NS57; -.
DR STRING; 10090.ENSMUSP00000068516; -.
DR iPTMnet; Q6NS57; -.
DR PhosphoSitePlus; Q6NS57; -.
DR PaxDb; Q6NS57; -.
DR PRIDE; Q6NS57; -.
DR ProteomicsDB; 291991; -. [Q6NS57-1]
DR ProteomicsDB; 291992; -. [Q6NS57-2]
DR DNASU; 26390; -.
DR GeneID; 26390; -.
DR KEGG; mmu:26390; -.
DR UCSC; uc008lux.2; mouse. [Q6NS57-2]
DR CTD; 23005; -.
DR MGI; MGI:1347004; Mapkbp1.
DR eggNOG; KOG1408; Eukaryota.
DR InParanoid; Q6NS57; -.
DR OrthoDB; 1017450at2759; -.
DR PhylomeDB; Q6NS57; -.
DR TreeFam; TF323254; -.
DR BioGRID-ORCS; 26390; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mapkbp1; mouse.
DR PRO; PR:Q6NS57; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6NS57; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1503
FT /note="Mitogen-activated protein kinase-binding protein 1"
FT /id="PRO_0000334159"
FT REPEAT 89..130
FT /note="WD 1"
FT REPEAT 133..174
FT /note="WD 2"
FT REPEAT 176..214
FT /note="WD 3"
FT REPEAT 271..310
FT /note="WD 4"
FT REPEAT 337..376
FT /note="WD 5"
FT REPEAT 382..431
FT /note="WD 6"
FT REPEAT 472..511
FT /note="WD 7"
FT REPEAT 514..556
FT /note="WD 8"
FT REPEAT 560..601
FT /note="WD 9"
FT REPEAT 609..648
FT /note="WD 10"
FT REPEAT 654..693
FT /note="WD 11"
FT REPEAT 696..735
FT /note="WD 12"
FT REGION 745..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1045
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60336"
FT VAR_SEQ 274
FT /note="R -> RNTDSFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10471813"
FT /id="VSP_033636"
FT CONFLICT 59
FT /note="D -> E (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="S -> P (in Ref. 1; BAA85449 and 2; CAM21732/
FT CAM22679)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="P -> L (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="V -> E (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 740..742
FT /note="AEL -> RER (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="G -> A (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="H -> D (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="H -> R (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="H -> L (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1090
FT /note="Q -> R (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1103
FT /note="S -> L (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1107..1119
FT /note="EPSLSSSGLALTS -> YGPPHMALLT (in Ref. 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="H -> R (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="Q -> R (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1267
FT /note="V -> A (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310
FT /note="A -> T (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1321..1324
FT /note="VSLG -> REPR (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359
FT /note="A -> R (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1370..1371
FT /note="GP -> A (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1432
FT /note="Y -> C (in Ref. 1; BAA85449 and 4; BAC65605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1452
FT /note="S -> P (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="G -> A (in Ref. 1; BAA85449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1503 AA; 162892 MW; F727BB02C687084B CRC64;
MMAGEGSTIT SRIKNLLRSP SIKLRRSKAG NRREDLSSKV TLEKVLGVTV SGGRGLACDP
RSGLVAYSAG CVVVLFNPRK HKQHHILNSS RKTITALAFS PDGKYLVTGE SGHMPAVRVW
DVAERSQVAE LQEHKYGVAC VAFSPSAKYI VSVGYQHDMI VNVWAWKKNI VVASNKVSSR
VTAVSFSEDC SYFVTAGNRH IKFWYLDDSK TSKVNATVPL LGRSGLLGEL RNNLFTDVAC
GRGEKADSTF CITSSGLLCE FSDRRLLDKW VELRTTVAHC ISVTQEYIFC GCADGTVRLF
NPSNLHFLST LPRPHALGTD IASITEASRL FSGGVNARYP DTIALTFDPT NQWLSCVYND
HSIYVWDVRD PKKVGKVYSA LYHSSCVWSV EVYPEIKDSH QACLPPSSFI TCSSDNTIRL
WNTESSGVHG STLHRNILSN DLIKIIYVDG NTQALLDTEL PGGDKADGSL MDPRVGIRSV
CISPNGQHLA SGDRMGTLRI HELQSLSEML KVEAHDSEIL CLEYSKPDTG LKLLASASRD
RLIHVLDAGR EYSLQQTLDE HSSSITAVKF AASDGQVRMI SCGADKSIYF RTAQKSGEGV
QFTRTHHVVR KTTLYDMDVE PSWKYTAIGC QDRNIRIFNI SSGKQKKLFK GSQGEDGTLI
KVQTDPSGIY IATSCSDKNL SIFDFSSGEC VATMFGHSEI VTGMKFSNDC KHLISVSGDS
CIFVWRLSSE MTISMRQRLA ELRQRQRGIK QQGPTSPQRA SGAKQHHAPV VPPSGPALSS
DSDKEGEDEG TEEEELPALP ILSKSTKKEL ASGSSPALLR SLSHWEMSRA QETMEYLDPA
PVANTGPKRR GRWAQPGVEL SVRSMLDLRQ IETLAPSPRG PSQDSLAVSP AGPGKHGPQG
PELSCVSQNE RAPRLQTSQP CSCPHIIQLL SQEEGVFAQD LEPAPIEDGI VYPEPSDSPT
MDTSAFQVQA PTGGSLGRMY PGSRGSEKHS PDSACSVDYS SSRLSSPEHP NEDSESTEPL
SVDGISSDLE EPAEGDEDEE EEGGTGLCGL QEGGPHTPDQ EQFLKQHFET LANGTAPGGP
ARVLERTESQ SISSRFLLQV QTSPLREPSL SSSGLALTSR PDQVSQVSGE QLKGSGATPP
GAPPEMEPSS GNSGPKQVAP VLLTRRHNNL DNSWASKKMA ATRPLAGLQK AQSVHSLVPQ
DEVPSSRPLL FQEAETQGSL GSLPQAGGCS SQPHSYQNHT TSSMAKLARS ISVGENPGLA
TEPQAPVPIR ISPFNKLALP SRAHLVLDIP KPLPDRPTLT TFSPVSKGLA HNETEQSGPL
VSLGKAHTTV EKHSCLGEGT THKSRTECQA YPGPNHPCAQ QLPVNNLLQG PESLQPLSPE
KTRNPVESSR PGVALSQDSE LALSLQQCEQ LVAELQGNVR QAVELYRAVT SYKTPSAEQS
HITRLLRDTF SSVRQELEVL AGAVLSSPGG SPGAVGAEQT QALLEQYSEL LLRAVERRME
RRL
