MBIP1_MOUSE
ID MBIP1_MOUSE Reviewed; 341 AA.
AC Q99LQ1; Q3TBM3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=MAP3K12-binding inhibitory protein 1;
DE AltName: Full=MAPK upstream kinase-binding inhibitory protein;
DE Short=MUK-binding inhibitory protein;
GN Name=Mbip;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Inhibits the MAP3K12 activity to induce the activation of the
CC JNK/SAPK pathway. Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4. {ECO:0000250}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC In the complex, it probably interacts directly with KAT2A, KAT14 and
CC WDR5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shows a cytoplasmic localization when co-expressed with MAP3K12.
CC {ECO:0000250}.
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DR EMBL; AK077125; BAC36628.1; -; mRNA.
DR EMBL; AK154318; BAE32511.1; -; mRNA.
DR EMBL; AK171164; BAE42286.1; -; mRNA.
DR EMBL; BC002277; AAH02277.1; -; mRNA.
DR CCDS; CCDS25920.1; -.
DR RefSeq; NP_663417.1; NM_145442.2.
DR AlphaFoldDB; Q99LQ1; -.
DR SMR; Q99LQ1; -.
DR BioGRID; 229926; 3.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q99LQ1; 3.
DR MINT; Q99LQ1; -.
DR STRING; 10090.ENSMUSP00000021416; -.
DR iPTMnet; Q99LQ1; -.
DR PhosphoSitePlus; Q99LQ1; -.
DR EPD; Q99LQ1; -.
DR jPOST; Q99LQ1; -.
DR MaxQB; Q99LQ1; -.
DR PaxDb; Q99LQ1; -.
DR PeptideAtlas; Q99LQ1; -.
DR PRIDE; Q99LQ1; -.
DR ProteomicsDB; 287320; -.
DR Antibodypedia; 166; 146 antibodies from 26 providers.
DR DNASU; 217588; -.
DR Ensembl; ENSMUST00000021416; ENSMUSP00000021416; ENSMUSG00000021028.
DR GeneID; 217588; -.
DR KEGG; mmu:217588; -.
DR UCSC; uc007npc.2; mouse.
DR CTD; 51562; -.
DR MGI; MGI:1918320; Mbip.
DR VEuPathDB; HostDB:ENSMUSG00000021028; -.
DR eggNOG; ENOG502R8QG; Eukaryota.
DR GeneTree; ENSGT00510000047831; -.
DR HOGENOM; CLU_069631_0_0_1; -.
DR InParanoid; Q99LQ1; -.
DR OMA; HKSNSML; -.
DR OrthoDB; 1543738at2759; -.
DR PhylomeDB; Q99LQ1; -.
DR TreeFam; TF331763; -.
DR BioGRID-ORCS; 217588; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Mbip; mouse.
DR PRO; PR:Q99LQ1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99LQ1; protein.
DR Bgee; ENSMUSG00000021028; Expressed in humerus cartilage element and 256 other tissues.
DR ExpressionAtlas; Q99LQ1; baseline and differential.
DR Genevisible; Q99LQ1; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR InterPro; IPR026062; MBIP.
DR PANTHER; PTHR23404:SF3; PTHR23404:SF3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..341
FT /note="MAP3K12-binding inhibitory protein 1"
FT /id="PRO_0000096270"
FT REGION 170..341
FT /note="Interaction with MAP3K12"
FT REGION 269..283
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000255"
FT REGION 312..327
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000255"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT MOD_RES 299
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NS73"
SQ SEQUENCE 341 AA; 38333 MW; C83C4DDA6CBABCDA CRC64;
MAAAAELSSS SGSERSLEQC SSPLLTREVL CEVFRSLHTL TRQLNLRDDV VKITIDWNRL
QSLSASQPAL LLTALEQHVL YLQPFLAKLQ SLMKENSTAT EIRQTEAETK SELRAIHPTE
DLQDEGKPKD CDVGDVKKTQ NLFDPEVVQI KAGKAEIDRR ISAFIERKQA EINENNVREF
CNVIDCNQEN SCARTDAVFT PYPGFKSHVK VSRVVNTYGP QTRPEGIAGS GHKPTGMLRD
CGNQAVEERL QNIEAHLRLQ TGGPVPRDIY QRIKKLEDKI LELEGISPEY FQSVNFSGKR
RKVQPPQQNY SLAELDEKIS ALKRALLRKS READSMAAHL P
