MABP1_HUMAN
ID MABP1_HUMAN Reviewed; 1514 AA.
AC O60336; A6NM93; A8K8P9; Q14CB5; Q14CD8; Q49AJ8; Q5W9G9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 169.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT PRO-1240.
RC TISSUE=Brain;
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist in the
RT human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-1240.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND VARIANT PRO-1240.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP VARIANT PRO-1240.
RC TISSUE=Testis;
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NOD2.
RX PubMed=22700971; DOI=10.1074/jbc.m112.355545;
RA Lecat A., Di Valentin E., Somja J., Jourdan S., Fillet M., Kufer T.A.,
RA Habraken Y., Sadzot C., Louis E., Delvenne P., Piette J., Legrand-Poels S.;
RT "The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a
RT negative regulator of NOD2 protein signaling by inhibiting its
RT oligomerization process.";
RL J. Biol. Chem. 287:29213-29226(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP SUBUNIT, AND INTERACTION WITH WDR62.
RX PubMed=23341463; DOI=10.1074/jbc.m112.422055;
RA Cohen-Katsenelson K., Wasserman T., Darlyuk-Saadon I., Rabner A.,
RA Glaser F., Aronheim A.;
RT "Identification and analysis of a novel dimerization domain shared by
RT various members of c-Jun N-terminal kinase (JNK) scaffold proteins.";
RL J. Biol. Chem. 288:7294-7304(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH WDR62 AND MAPK9,
RP INVOLVEMENT IN NPHP20, VARIANT NPHP20 GLN-544, AND CHARACTERIZATION OF
RP VARIANT NPHP20 GLN-544.
RX PubMed=28089251; DOI=10.1016/j.ajhg.2016.12.011;
RA Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A., Filhol E.,
RA Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y., Silbermann F.,
RA Henry C., Krug P., Bole-Feysot C., Nitschke P., Joly D., Nicoud P.,
RA Paget A., Haugland H., Brackmann D., Ahmet N., Sandford R., Cengiz N.,
RA Knappskog P.M., Boman H., Linghu B., Yang F., Oakeley E.J.,
RA Saint Mezard P., Sailer A.W., Johansson S., Roedahl E., Saunier S.,
RA Hildebrandt F., Benmerah A.;
RT "Mutations in MAPKBP1 cause juvenile or late-onset cilia-independent
RT nephronophthisis.";
RL Am. J. Hum. Genet. 100:323-333(2017).
RN [14]
RP ERRATUM OF PUBMED:28089251.
RX PubMed=28157543; DOI=10.1016/j.ajhg.2017.01.025;
RA Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A., Filhol E.,
RA Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y., Silbermann F.,
RA Henry C., Krug P., Bole-Feysot C., Nitschke P., Joly D., Nicoud P.,
RA Paget A., Haugland H., Brackmann D., Ahmet N., Sandford R., Cengiz N.,
RA Knappskog P.M., Boman H., Linghu B., Yang F., Oakeley E.J.,
RA Saint Mezard P., Sailer A.W., Johansson S., Roedahl E., Saunier S.,
RA Hildebrandt F., Benmerah A.;
RL Am. J. Hum. Genet. 100:372-372(2017).
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 (PubMed:22700971). Involved in JNK
CC signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q6NS57,
CC ECO:0000269|PubMed:22700971}.
CC -!- SUBUNIT: Can form homodimers (via C-terminus) (PubMed:23341463).
CC Interacts (via C-terminus) with WDR62 (via C-terminus)
CC (PubMed:23341463, PubMed:28089251). Interacts with MAPK9
CC (PubMed:28089251). Interacts (via N-terminus) with NOD2; the
CC interaction is enhanced in presence of muramyl dipeptide (MDP)
CC (PubMed:22700971). Interacts with MAPK10 (By similarity).
CC {ECO:0000250|UniProtKB:Q6NS57, ECO:0000269|PubMed:22700971,
CC ECO:0000269|PubMed:23341463, ECO:0000269|PubMed:28089251}.
CC -!- INTERACTION:
CC O60336; O43184-4: ADAM12; NbExp=3; IntAct=EBI-947402, EBI-12006944;
CC O60336; Q6UY14-3: ADAMTSL4; NbExp=6; IntAct=EBI-947402, EBI-10173507;
CC O60336; Q9NP73-4: ALG13; NbExp=3; IntAct=EBI-947402, EBI-10186621;
CC O60336; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-947402, EBI-751587;
CC O60336; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-947402, EBI-3867333;
CC O60336; O15353: FOXN1; NbExp=3; IntAct=EBI-947402, EBI-11319000;
CC O60336; O76003: GLRX3; NbExp=6; IntAct=EBI-947402, EBI-374781;
CC O60336; P49639: HOXA1; NbExp=5; IntAct=EBI-947402, EBI-740785;
CC O60336; Q14145: KEAP1; NbExp=3; IntAct=EBI-947402, EBI-751001;
CC O60336; Q5T749: KPRP; NbExp=5; IntAct=EBI-947402, EBI-10981970;
CC O60336; Q15323: KRT31; NbExp=6; IntAct=EBI-947402, EBI-948001;
CC O60336; O76011: KRT34; NbExp=3; IntAct=EBI-947402, EBI-1047093;
CC O60336; Q92764: KRT35; NbExp=3; IntAct=EBI-947402, EBI-1058674;
CC O60336; O76015: KRT38; NbExp=3; IntAct=EBI-947402, EBI-1047263;
CC O60336; Q6A162: KRT40; NbExp=3; IntAct=EBI-947402, EBI-10171697;
CC O60336; O43790: KRT86; NbExp=3; IntAct=EBI-947402, EBI-9996498;
CC O60336; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-947402, EBI-11959885;
CC O60336; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-947402, EBI-11749135;
CC O60336; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-947402, EBI-10172290;
CC O60336; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-947402, EBI-10171774;
CC O60336; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-947402, EBI-10172052;
CC O60336; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-947402, EBI-11953334;
CC O60336; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-947402, EBI-3957672;
CC O60336; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-947402, EBI-9996449;
CC O60336; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-947402, EBI-751260;
CC O60336; Q9BQ66: KRTAP4-12; NbExp=6; IntAct=EBI-947402, EBI-739863;
CC O60336; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-947402, EBI-10250562;
CC O60336; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-947402, EBI-11987425;
CC O60336; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-947402, EBI-3958099;
CC O60336; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-947402, EBI-1044640;
CC O60336; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-947402, EBI-1043191;
CC O60336; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-947402, EBI-10185730;
CC O60336; Q99750: MDFI; NbExp=6; IntAct=EBI-947402, EBI-724076;
CC O60336; P50222: MEOX2; NbExp=3; IntAct=EBI-947402, EBI-748397;
CC O60336; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947402, EBI-16439278;
CC O60336; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-947402, EBI-10174029;
CC O60336; P15173: MYOG; NbExp=3; IntAct=EBI-947402, EBI-3906629;
CC O60336; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-947402, EBI-945833;
CC O60336; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-947402, EBI-22310682;
CC O60336; O15496: PLA2G10; NbExp=3; IntAct=EBI-947402, EBI-726466;
CC O60336; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-947402, EBI-750734;
CC O60336; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-947402, EBI-2340624;
CC O60336; O76081: RGS20; NbExp=3; IntAct=EBI-947402, EBI-1052678;
CC O60336; O76081-6: RGS20; NbExp=3; IntAct=EBI-947402, EBI-10178530;
CC O60336; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-947402, EBI-747107;
CC O60336; O43597: SPRY2; NbExp=3; IntAct=EBI-947402, EBI-742487;
CC O60336; O43610: SPRY3; NbExp=3; IntAct=EBI-947402, EBI-12290641;
CC O60336; Q99081: TCF12; NbExp=3; IntAct=EBI-947402, EBI-722877;
CC O60336; P15884: TCF4; NbExp=3; IntAct=EBI-947402, EBI-533224;
CC O60336; P15884-3: TCF4; NbExp=3; IntAct=EBI-947402, EBI-13636688;
CC O60336; Q96M29: TEKT5; NbExp=3; IntAct=EBI-947402, EBI-10239812;
CC O60336; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-947402, EBI-742397;
CC O60336; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-947402, EBI-11523345;
CC O60336; P14373: TRIM27; NbExp=3; IntAct=EBI-947402, EBI-719493;
CC O60336; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-947402, EBI-5235829;
CC O60336; Q15654: TRIP6; NbExp=3; IntAct=EBI-947402, EBI-742327;
CC O60336; P62699: YPEL5; NbExp=3; IntAct=EBI-947402, EBI-11721624;
CC O60336; Q7Z783; NbExp=3; IntAct=EBI-947402, EBI-9088990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22700971,
CC ECO:0000269|PubMed:28089251}. Nucleus {ECO:0000269|PubMed:22700971}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:28089251}.
CC Note=Not detected in the cilium. Localized around the poles of the
CC mitotic spindle from prophase to anaphase in mitotic cells.
CC {ECO:0000269|PubMed:28089251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O60336-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60336-2; Sequence=VSP_033633, VSP_033634;
CC Name=3;
CC IsoId=O60336-3; Sequence=VSP_033632, VSP_033635;
CC Name=4;
CC IsoId=O60336-4; Sequence=VSP_033629;
CC Name=5;
CC IsoId=O60336-5; Sequence=VSP_033630, VSP_033631;
CC Name=6;
CC IsoId=O60336-6; Sequence=VSP_033633;
CC -!- TISSUE SPECIFICITY: Expressed in intestinal mucosa, where it is
CC detected in epithelial cells, endothelial cells, smooth muscle cells
CC and immune cells, such as lymphocytes (PubMed:22700971). Expressed in
CC kidney (PubMed:28089251). {ECO:0000269|PubMed:22700971,
CC ECO:0000269|PubMed:28089251}.
CC -!- DOMAIN: The N-terminal WD40 domain is necessary for the interaction
CC with NOD2 and down-regulation of NOD2 function.
CC {ECO:0000269|PubMed:22700971}.
CC -!- DISEASE: Nephronophthisis 20 (NPHP20) [MIM:617271]: A form of
CC nephronophthisis, an autosomal recessive chronic tubulo-interstitial
CC nephritis that progresses to end-stage renal failure. Some patients
CC have cystic kidneys of normal size and no extrarenal manifestations,
CC whereas others have enlarged renal size and severe extrarenal defects,
CC including hypertrophic obstructive cardiomyopathy, aortic stenosis,
CC pulmonary stenosis, patent ductus arteriosus, situs inversus, and
CC periportal liver fibrosis. NPHP20 patients do not show extrarenal
CC manifestations or evidence of a ciliopathy, such as situs inversus or
CC polydactyly. {ECO:0000269|PubMed:28089251}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25522.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB177850; BAD66828.1; -; mRNA.
DR EMBL; AB011168; BAA25522.2; ALT_INIT; mRNA.
DR EMBL; AK292414; BAF85103.1; -; mRNA.
DR EMBL; AL833267; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC020659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92516.1; -; Genomic_DNA.
DR EMBL; BC036660; AAH36660.1; -; mRNA.
DR EMBL; BC113983; AAI13984.1; -; mRNA.
DR EMBL; BC114493; AAI14494.1; -; mRNA.
DR CCDS; CCDS32201.1; -. [O60336-6]
DR CCDS; CCDS45239.1; -. [O60336-1]
DR CCDS; CCDS58359.1; -. [O60336-2]
DR PIR; T00270; T00270.
DR RefSeq; NP_001122080.1; NM_001128608.1. [O60336-1]
DR RefSeq; NP_001252540.1; NM_001265611.1. [O60336-2]
DR RefSeq; NP_055809.2; NM_014994.2. [O60336-6]
DR AlphaFoldDB; O60336; -.
DR SMR; O60336; -.
DR BioGRID; 116650; 70.
DR ELM; O60336; -.
DR IntAct; O60336; 61.
DR MINT; O60336; -.
DR STRING; 9606.ENSP00000393099; -.
DR GlyGen; O60336; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60336; -.
DR PhosphoSitePlus; O60336; -.
DR BioMuta; MAPKBP1; -.
DR EPD; O60336; -.
DR jPOST; O60336; -.
DR MassIVE; O60336; -.
DR MaxQB; O60336; -.
DR PaxDb; O60336; -.
DR PeptideAtlas; O60336; -.
DR PRIDE; O60336; -.
DR ProteomicsDB; 49357; -. [O60336-1]
DR ProteomicsDB; 49358; -. [O60336-2]
DR ProteomicsDB; 49359; -. [O60336-3]
DR ProteomicsDB; 49360; -. [O60336-4]
DR ProteomicsDB; 49361; -. [O60336-5]
DR ProteomicsDB; 49362; -. [O60336-6]
DR Antibodypedia; 23379; 96 antibodies from 22 providers.
DR DNASU; 23005; -.
DR Ensembl; ENST00000456763.6; ENSP00000393099.2; ENSG00000137802.14. [O60336-1]
DR Ensembl; ENST00000457542.7; ENSP00000397570.2; ENSG00000137802.14. [O60336-6]
DR Ensembl; ENST00000514566.5; ENSP00000426154.1; ENSG00000137802.14. [O60336-2]
DR GeneID; 23005; -.
DR KEGG; hsa:23005; -.
DR MANE-Select; ENST00000457542.7; ENSP00000397570.2; NM_014994.3; NP_055809.2. [O60336-6]
DR UCSC; uc001zoj.4; human. [O60336-1]
DR CTD; 23005; -.
DR DisGeNET; 23005; -.
DR GeneCards; MAPKBP1; -.
DR HGNC; HGNC:29536; MAPKBP1.
DR HPA; ENSG00000137802; Low tissue specificity.
DR MalaCards; MAPKBP1; -.
DR MIM; 616786; gene.
DR MIM; 617271; phenotype.
DR neXtProt; NX_O60336; -.
DR OpenTargets; ENSG00000137802; -.
DR Orphanet; 93592; Juvenile nephronophthisis.
DR Orphanet; 93589; Late-onset nephronophthisis.
DR PharmGKB; PA142671479; -.
DR VEuPathDB; HostDB:ENSG00000137802; -.
DR eggNOG; KOG1408; Eukaryota.
DR GeneTree; ENSGT00940000160664; -.
DR HOGENOM; CLU_002067_3_0_1; -.
DR InParanoid; O60336; -.
DR OMA; NEGCGAN; -.
DR OrthoDB; 1017450at2759; -.
DR PhylomeDB; O60336; -.
DR TreeFam; TF323254; -.
DR PathwayCommons; O60336; -.
DR SignaLink; O60336; -.
DR BioGRID-ORCS; 23005; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; MAPKBP1; human.
DR GenomeRNAi; 23005; -.
DR Pharos; O60336; Tbio.
DR PRO; PR:O60336; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O60336; protein.
DR Bgee; ENSG00000137802; Expressed in right hemisphere of cerebellum and 167 other tissues.
DR ExpressionAtlas; O60336; baseline and differential.
DR Genevisible; O60336; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
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; 7.
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 Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Nephronophthisis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1514
FT /note="Mitogen-activated protein kinase-binding protein 1"
FT /id="PRO_0000334158"
FT REPEAT 88..129
FT /note="WD 1"
FT REPEAT 132..173
FT /note="WD 2"
FT REPEAT 175..213
FT /note="WD 3"
FT REPEAT 276..315
FT /note="WD 4"
FT REPEAT 342..381
FT /note="WD 5"
FT REPEAT 387..436
FT /note="WD 6"
FT REPEAT 477..516
FT /note="WD 7"
FT REPEAT 519..561
FT /note="WD 8"
FT REPEAT 565..606
FT /note="WD 9"
FT REPEAT 614..653
FT /note="WD 10"
FT REPEAT 659..698
FT /note="WD 11"
FT REPEAT 701..740
FT /note="WD 12"
FT REGION 748..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1050
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..499
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033629"
FT VAR_SEQ 214..215
FT /note="NA -> RC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033630"
FT VAR_SEQ 216..1514
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033631"
FT VAR_SEQ 274..396
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607"
FT /id="VSP_033632"
FT VAR_SEQ 274..279
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_033633"
FT VAR_SEQ 1134..1410
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033634"
FT VAR_SEQ 1411..1412
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607"
FT /id="VSP_033635"
FT VARIANT 204
FT /note="Y -> S (in dbSNP:rs4354909)"
FT /id="VAR_043343"
FT VARIANT 313
FT /note="L -> V (in dbSNP:rs1201689)"
FT /id="VAR_043344"
FT VARIANT 544
FT /note="R -> Q (in NPHP20; unknown pathological
FT significance; no effect on localization at the spindle
FT pole; no effect on interaction with WDR62; no effect on
FT interaction with MAPK9; dbSNP:rs1057519305)"
FT /evidence="ECO:0000269|PubMed:28089251"
FT /id="VAR_077958"
FT VARIANT 1240
FT /note="R -> P (in dbSNP:rs3959569)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15491607, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9628581"
FT /id="VAR_043345"
FT CONFLICT 843
FT /note="P -> S (in Ref. 8; AAH36660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1444
FT /note="K -> R (in Ref. 5; AL833267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1514 AA; 163818 MW; 13FD125E44CABBFD CRC64;
MAVEGSTITS RIKNLLRSPS IKLRRSKAGN RREDLSSKVT LEKVLGITVS GGRGLACDPR
SGLVAYPAGC VVVLFNPRKH KQHHILNSSR KTITALAFSP DGKYLVTGES GHMPAVRVWD
VAEHSQVAEL QEHKYGVACV AFSPSAKYIV SVGYQHDMIV NVWAWKKNIV VASNKVSSRV
TAVSFSEDCS YFVTAGNRHI KFWYLDDSKT SKVNATVPLL GRSGLLGELR NNLFTDVACG
RGKKADSTFC ITSSGLLCEF SDRRLLDKWV ELRNIDSFTT TVAHCISVSQ DYIFCGCADG
TVRLFNPSNL HFLSTLPRPH ALGTDIASVT EASRLFSGVA NARYPDTIAL TFDPTNQWLS
CVYNDHSIYV WDVRDPKKVG KVYSALYHSS CVWSVEVYPE VKDSNQACLP PSSFITCSSD
NTIRLWNTES SGVHGSTLHR NILSSDLIKI IYVDGNTQAL LDTELPGGDK ADASLLDPRV
GIRSVCVSPN GQHLASGDRM GTLRVHELQS LSEMLKVEAH DSEILCLEYS KPDTGLKLLA
SASRDRLIHV LDAGREYSLQ QTLDEHSSSI TAVKFAASDG QVRMISCGAD KSIYFRTAQK
SGDGVQFTRT HHVVRKTTLY DMDVEPSWKY TAIGCQDRNI RIFNISSGKQ KKLFKGSQGE
DGTLIKVQTD PSGIYIATSC SDKNLSIFDF SSGECVATMF GHSEIVTGMK FSNDCKHLIS
VSGDSCIFVW RLSSEMTISM RQRLAELRQR QRGGKQQGPS SPQRASGPNR HQAPSMLSPG
PALSSDSDKE GEDEGTEEEL PALPVLAKST KKALASVPSP ALPRSLSHWE MSRAQESVGF
LDPAPAANPG PRRRGRWVQP GVELSVRSML DLRQLETLAP SLQDPSQDSL AIIPSGPRKH
GQEALETSLT SQNEKPPRPQ ASQPCSYPHI IRLLSQEEGV FAQDLEPAPI EDGIVYPEPS
DNPTMDTSEF QVQAPARGTL GRVYPGSRSS EKHSPDSACS VDYSSSCLSS PEHPTEDSES
TEPLSVDGIS SDLEEPAEGD EEEEEEEGGM GPYGLQEGSP QTPDQEQFLK QHFETLASGA
APGAPVQVPE RSESRSISSR FLLQVQTRPL REPSPSSSSL ALMSRPAQVP QASGEQPRGN
GANPPGAPPE VEPSSGNPSP QQAASVLLPR CRLNPDSSWA PKRVATASPF SGLQKAQSVH
SLVPQERHEA SLQAPSPGAL LSREIEAQDG LGSLPPADGR PSRPHSYQNP TTSSMAKISR
SISVGENLGL VAEPQAHAPI RVSPLSKLAL PSRAHLVLDI PKPLPDRPTL AAFSPVTKGR
APGEAEKPGF PVGLGKAHST TERWACLGEG TTPKPRTECQ AHPGPSSPCA QQLPVSSLFQ
GPENLQPPPP EKTPNPMECT KPGAALSQDS EPAVSLEQCE QLVAELRGSV RQAVRLYHSV
AGCKMPSAEQ SRIAQLLRDT FSSVRQELEA VAGAVLSSPG SSPGAVGAEQ TQALLEQYSE
LLLRAVERRM ERKL
