MTBP_HUMAN
ID MTBP_HUMAN Reviewed; 904 AA.
AC Q96DY7; B4DUR5; Q9HA89;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mdm2-binding protein;
DE Short=hMTBP;
GN Name=MTBP;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-141 (ISOFORM 1).
RC TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [5]
RP FUNCTION, AND INTERACTION WITH MDM2.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703 AND SER-707, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597 AND SER-639, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Inhibits cell migration in vitro and suppresses the invasive
CC behavior of tumor cells (By similarity). May play a role in MDM2-
CC dependent p53/TP53 homeostasis in unstressed cells. Inhibits
CC autoubiquitination of MDM2, thereby enhancing MDM2 stability. This
CC promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent
CC degradation. {ECO:0000250, ECO:0000269|PubMed:15632057}.
CC -!- SUBUNIT: Interacts with MDM2. {ECO:0000269|PubMed:15632057}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DY7-3; Sequence=VSP_056108, VSP_056109;
CC -!- SIMILARITY: Belongs to the MTBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13965.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. May result from internal priming due to genomic poly-A tracts.; Evidence={ECO:0000305};
CC Sequence=EAW92007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK022122; BAB13965.1; ALT_SEQ; mRNA.
DR EMBL; AK300762; BAG62427.1; -; mRNA.
DR EMBL; AC105142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW92006.1; -; Genomic_DNA.
DR EMBL; CH471060; EAW92007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC013136; AAH13136.1; -; mRNA.
DR CCDS; CCDS6333.1; -. [Q96DY7-1]
DR RefSeq; NP_071328.2; NM_022045.4. [Q96DY7-1]
DR AlphaFoldDB; Q96DY7; -.
DR BioGRID; 117988; 29.
DR IntAct; Q96DY7; 5.
DR STRING; 9606.ENSP00000303398; -.
DR iPTMnet; Q96DY7; -.
DR PhosphoSitePlus; Q96DY7; -.
DR BioMuta; MTBP; -.
DR DMDM; 74731509; -.
DR EPD; Q96DY7; -.
DR jPOST; Q96DY7; -.
DR MassIVE; Q96DY7; -.
DR MaxQB; Q96DY7; -.
DR PaxDb; Q96DY7; -.
DR PeptideAtlas; Q96DY7; -.
DR PRIDE; Q96DY7; -.
DR ProteomicsDB; 5205; -.
DR ProteomicsDB; 76343; -. [Q96DY7-1]
DR Antibodypedia; 13747; 283 antibodies from 30 providers.
DR DNASU; 27085; -.
DR Ensembl; ENST00000305949.6; ENSP00000303398.1; ENSG00000172167.8. [Q96DY7-1]
DR Ensembl; ENST00000523373.5; ENSP00000430771.1; ENSG00000172167.8. [Q96DY7-3]
DR GeneID; 27085; -.
DR KEGG; hsa:27085; -.
DR MANE-Select; ENST00000305949.6; ENSP00000303398.1; NM_022045.5; NP_071328.2.
DR UCSC; uc003ypc.3; human. [Q96DY7-1]
DR CTD; 27085; -.
DR DisGeNET; 27085; -.
DR GeneCards; MTBP; -.
DR HGNC; HGNC:7417; MTBP.
DR HPA; ENSG00000172167; Low tissue specificity.
DR MIM; 605927; gene.
DR neXtProt; NX_Q96DY7; -.
DR OpenTargets; ENSG00000172167; -.
DR PharmGKB; PA31224; -.
DR VEuPathDB; HostDB:ENSG00000172167; -.
DR eggNOG; ENOG502RGBH; Eukaryota.
DR GeneTree; ENSGT00390000003305; -.
DR HOGENOM; CLU_923010_0_0_1; -.
DR InParanoid; Q96DY7; -.
DR OMA; EIHFGTE; -.
DR OrthoDB; 1334548at2759; -.
DR PhylomeDB; Q96DY7; -.
DR TreeFam; TF331503; -.
DR PathwayCommons; Q96DY7; -.
DR SignaLink; Q96DY7; -.
DR BioGRID-ORCS; 27085; 719 hits in 1094 CRISPR screens.
DR ChiTaRS; MTBP; human.
DR GenomeRNAi; 27085; -.
DR Pharos; Q96DY7; Tbio.
DR PRO; PR:Q96DY7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96DY7; protein.
DR Bgee; ENSG00000172167; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; Q96DY7; baseline and differential.
DR Genevisible; Q96DY7; HS.
DR GO; GO:0000785; C:chromatin; IDA: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; IEA:Ensembl.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP: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; IBA:GO_Central.
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..904
FT /note="Mdm2-binding protein"
FT /id="PRO_0000323745"
FT REGION 19..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..904
FT /note="Interaction with MDM2"
FT /evidence="ECO:0000250"
FT REGION 754..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 326..329
FT /note="LGLT -> FTED (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056108"
FT VAR_SEQ 330..904
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056109"
SQ SEQUENCE 904 AA; 102193 MW; 753DF4A98AB62E4F CRC64;
MDRYLLLVIW GEGKFPSAAS REAEHGPEVS SGEGTENQPD FTAANVYHLL KRSISASINP
EDSTFPACSV GGIPGSKKWF FAVQAIYGFY QFCSSDWQEI HFDTEKDKIE DVLQTNIEEC
LGAVECFEEE DSNSRESLSL ADLYEEAAEN LHQLSDKLPA PGRAMVDIIL LLSDKDPPKL
KDYLPTVGAL KHLREWYSAK ITIAGNHCEI NCQKIAEYLS ANVVSLEDLR NVIDSKELWR
GKIQIWERKF GFEISFPEFC LKGVTLKNFS TSNLNTDFLA KKIIPSKDKN ILPKVFHYYG
PALEFVQMIK LSDLPSCYMS DIEFELGLTN STKQNSVLLL EQISSLCSKV GALFVLPCTI
SNILIPPPNQ LSSRKWKEYI AKKPKTISVP DVEVKGECSS YYLLLQGNGN RRCKATLIHS
ANQINGSFAL NLIHGKMKTK TEEAKLSFPF DLLSLPHFSG EQIVQREKQL ANVQVLALEE
CLKRRKLAKQ PETVSVAELK SLLVLTRKHF LDYFDAVIPK MILRKMDKIK TFNILNDFSP
VEPNSSSLME TNPLEWPERH VLQNLETFEK TKQKMRTGSL PHSSEQLLGH KEGPRDSITL
LDAKELLKYF TSDGLPIGDL QPLPIQKGEK TFVLTPELSP GKLQVLPFEK ASVCHYHGIE
YCLDDRKALE RDGGFSELQS RLIRYETQTT CTRESFPVPT VLSPLPSPVV SSDPGSVPDG
EVLQNELRTE VSRLKRRSKD LNCLYPRKRL VKSESSESLL SQTTGNSNHY HHHVTSRKPQ
TERSLPVTCP LVPIPSCETP KLATKTSSGQ KSMHESKTSR QIKESRSQKH TRILKEVVTE
TLKKHSITET HECFTACSQR LFEISKFYLK DLKTSRGLFE EMKKTANNNA VQVIDWVLEK
TSKK
