MTBP_MOUSE
ID MTBP_MOUSE Reviewed; 894 AA.
AC Q8BJS8; Q80VU3; Q8BTU9; Q8BTW0; Q99K25; Q9ER61;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Mdm2-binding protein;
DE Short=mMTBP;
GN Name=Mtbp;
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 1), FUNCTION, INTERACTION WITH MDM2,
RP AND TISSUE SPECIFICITY.
RX PubMed=10906133; DOI=10.1074/jbc.m004252200;
RA Boyd M.T., Vlatkovic N., Haines D.S.;
RT "A novel cellular protein (MTBP) binds to MDM2 and induces a G1 arrest that
RT is suppressed by MDM2.";
RL J. Biol. Chem. 275:31883-31890(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Embryo, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
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 FUNCTION.
RX PubMed=15632057; DOI=10.1128/mcb.25.2.545-553.2005;
RA Brady M., Vlatkovic N., Boyd M.T.;
RT "Regulation of p53 and MDM2 activity by MTBP.";
RL Mol. Cell. Biol. 25:545-553(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17906694; DOI=10.1038/sj.onc.1210827;
RA Iwakuma T., Tochigi Y., Van Pelt C.S., Caldwell L.C., Terzian T.,
RA Parant J.M., Chau G.P., Koch J.G., Eischen C.M., Lozano G.;
RT "Mtbp haploinsufficiency in mice increases tumor metastasis.";
RL Oncogene 27:1813-1820(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: May play a role in MDM2-dependent p53/TP53 homeostasis in
CC unstressed cells. Inhibits autoubiquitination of MDM2, thereby
CC enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of
CC p53/TP53 and its subsequent degradation. Inhibits cell migration in
CC vitro and suppresses the invasive behavior of tumor cells.
CC {ECO:0000269|PubMed:10906133, ECO:0000269|PubMed:15632057}.
CC -!- SUBUNIT: Interacts with MDM2. {ECO:0000269|PubMed:10906133}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BJS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJS8-2; Sequence=VSP_032106, VSP_032107;
CC Name=3;
CC IsoId=Q8BJS8-3; Sequence=VSP_032105;
CC -!- TISSUE SPECIFICITY: Expressed in small intestine and spleen at low
CC levels, in the ovary at intermediate levels and in the testis and
CC thymus at high levels. {ECO:0000269|PubMed:10906133}.
CC -!- DISRUPTION PHENOTYPE: Death between E3.5 and E7.5. Mice containing a
CC heterozygous deletion of this gene coupled with heterozygous deletion
CC of TP53 exhibit an increased incidence of metastatic tumors.
CC {ECO:0000269|PubMed:17906694}.
CC -!- SIMILARITY: Belongs to the MTBP family. {ECO:0000305}.
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DR EMBL; AJ278508; CAC07970.1; -; mRNA.
DR EMBL; AK080036; BAC37810.1; -; mRNA.
DR EMBL; AK088549; BAC40418.1; -; mRNA.
DR EMBL; AK088652; BAC40479.1; -; mRNA.
DR EMBL; AK133855; BAE21889.1; -; mRNA.
DR EMBL; BC005500; AAH05500.1; -; mRNA.
DR EMBL; BC052197; AAH52197.1; -; mRNA.
DR CCDS; CCDS27478.1; -. [Q8BJS8-1]
DR CCDS; CCDS49609.1; -. [Q8BJS8-2]
DR RefSeq; NP_001161722.1; NM_001168250.1. [Q8BJS8-2]
DR RefSeq; NP_598853.3; NM_134092.3. [Q8BJS8-1]
DR AlphaFoldDB; Q8BJS8; -.
DR STRING; 10090.ENSMUSP00000022998; -.
DR iPTMnet; Q8BJS8; -.
DR PhosphoSitePlus; Q8BJS8; -.
DR EPD; Q8BJS8; -.
DR jPOST; Q8BJS8; -.
DR MaxQB; Q8BJS8; -.
DR PaxDb; Q8BJS8; -.
DR PeptideAtlas; Q8BJS8; -.
DR PRIDE; Q8BJS8; -.
DR ProteomicsDB; 291360; -. [Q8BJS8-1]
DR ProteomicsDB; 291361; -. [Q8BJS8-2]
DR ProteomicsDB; 291362; -. [Q8BJS8-3]
DR Antibodypedia; 13747; 283 antibodies from 30 providers.
DR Ensembl; ENSMUST00000022998; ENSMUSP00000022998; ENSMUSG00000022369. [Q8BJS8-1]
DR Ensembl; ENSMUST00000169667; ENSMUSP00000128615; ENSMUSG00000022369. [Q8BJS8-3]
DR Ensembl; ENSMUST00000170046; ENSMUSP00000129396; ENSMUSG00000022369. [Q8BJS8-2]
DR GeneID; 105837; -.
DR KEGG; mmu:105837; -.
DR UCSC; uc007vsi.1; mouse. [Q8BJS8-1]
DR UCSC; uc011zsz.1; mouse. [Q8BJS8-2]
DR CTD; 27085; -.
DR MGI; MGI:2146005; Mtbp.
DR VEuPathDB; HostDB:ENSMUSG00000022369; -.
DR eggNOG; ENOG502RGBH; Eukaryota.
DR GeneTree; ENSGT00390000003305; -.
DR HOGENOM; CLU_017071_0_0_1; -.
DR InParanoid; Q8BJS8; -.
DR OMA; EIHFGTE; -.
DR OrthoDB; 1334548at2759; -.
DR PhylomeDB; Q8BJS8; -.
DR TreeFam; TF331503; -.
DR BioGRID-ORCS; 105837; 15 hits in 77 CRISPR screens.
DR ChiTaRS; Mtbp; mouse.
DR PRO; PR:Q8BJS8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BJS8; protein.
DR Bgee; ENSMUSG00000022369; Expressed in undifferentiated genital tubercle and 152 other tissues.
DR ExpressionAtlas; Q8BJS8; baseline and differential.
DR Genevisible; Q8BJS8; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IDA:MGI.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IEA:InterPro.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IDA:MGI.
DR InterPro; IPR039061; MTBP.
DR InterPro; IPR029418; MTBP_C.
DR InterPro; IPR029420; MTBP_central.
DR InterPro; IPR029421; MTBP_N.
DR PANTHER; PTHR14382; PTHR14382; 1.
DR Pfam; PF14920; MTBP_C; 1.
DR Pfam; PF14919; MTBP_mid; 1.
DR Pfam; PF14918; MTBP_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Growth arrest; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..894
FT /note="Mdm2-binding protein"
FT /id="PRO_0000323746"
FT REGION 515..894
FT /note="Interaction with MDM2"
FT /evidence="ECO:0000269|PubMed:10906133"
FT REGION 563..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DY7"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DY7"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DY7"
FT VAR_SEQ 1..373
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032105"
FT VAR_SEQ 623..629
FT /note="EKPFVLT -> IHQLVHV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032106"
FT VAR_SEQ 630..894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032107"
FT CONFLICT 120
FT /note="C -> R (in Ref. 1; CAC07970)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="L -> V (in Ref. 1; CAC07970)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="P -> R (in Ref. 1; CAC07970)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="L -> V (in Ref. 1; CAC07970)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="F -> L (in Ref. 1; CAC07970)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="K -> R (in Ref. 3; AAH52197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 100314 MW; 93528336ED081A27 CRC64;
MDRYLLLVTW REGKFRSVAG GEIEPGTEAT SLESTDKQPD LTATNIYHLL KRSISDSIHP
DDSTFPACSV GGTPHSRKWF FAVQAICGFY QFCSSDWQEI HFDAEKDKIE DVLQANIEEC
QSAVECFEED DSNSRESLPL ADLYEESAEN LHQLSDKLPA PGRAMIDIIL LPSDKDPPKL
KECLPIVGAL KHLKEWHSAK VIIAGSYCEI NCQKIAEYLS ASVVPLEEFR NAIDPRELWR
GEIQMRERKF GFEISFPEFC LKGVTPTNVS AYNLNTCFLA KKIASSKVFH YYGPALEFVQ
MIKLSDLPSC YMSDIEFELE VTGHCTRQNS MLLLEQISSL CGKVGALFVL PCTVSNVLIP
PPSQLASRKW KEYMAKKPKT ISVPDVAVKG EFSGYHLLLQ GMGKRKCRAT LLHSASQING
SFALSVIHGK MKTKAGEARP SFPFDFSSLP RFSEEQVLQR EKQLASFQVL ALKECLKRRK
AANQPEAFSA DELKSLLALT RERFLGHFDV LPTEAALAQT DTVKAAGVVN DDGTVEPYSS
SLMETNPLEW PERHVLQNLE TSEKAKQKMR TGSLPRSSEQ LLGHKEGPRD SLTLLDAKEL
LKYFTSDGLP VGDLQPLHIQ RGEKPFVLTP ELSPGKLQVL PFEKASECHY HGIEYCLDDQ
KALERDGGFS ELQSRLIRYE TQTTCTRDSF PVPTVLSPLP SPAVLSEPQS VPEGEALQGE
LRTEVSGLKR RSKDPSCLYP QKRLTRSESS DCLPSQASCN SNHHHHTGKP RKPQAERCVS
GLPLPGREAS KDTSKTSSGQ KRAHESKSSK QMKESRSQKH TRMLKEVVKD TLKRHHITEA
HESFTACSQR LFDISKFYLK DLKTSRGLFE EMKKTANNNV VQVIEWVVEK MSKK
