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Q96DY7 (MTBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mdm2-binding protein

Short name=hMTBP
Gene names
Name:MTBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells By similarity. May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2, thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. Ref.4

Subunit structure

Interacts with MDM2. Ref.4

Sequence similarities

Belongs to the MTBP family.

Sequence caution

The sequence BAB13965.1 differs from that shown. Reason: Probable cloning artifact. May result from internal priming due to genomic poly-A tracts.

The sequence EAW92007.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 904904Mdm2-binding protein
PRO_0000323745

Regions

Region521 – 904384Interaction with MDM2 By similarity

Amino acid modifications

Modified residue6391Phosphoserine Ref.5 Ref.8
Modified residue7031Phosphoserine Ref.7
Modified residue7071Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q96DY7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 753DF4A98AB62E4F

FASTA904102,193
        10         20         30         40         50         60 
MDRYLLLVIW GEGKFPSAAS REAEHGPEVS SGEGTENQPD FTAANVYHLL KRSISASINP 

        70         80         90        100        110        120 
EDSTFPACSV GGIPGSKKWF FAVQAIYGFY QFCSSDWQEI HFDTEKDKIE DVLQTNIEEC 

       130        140        150        160        170        180 
LGAVECFEEE DSNSRESLSL ADLYEEAAEN LHQLSDKLPA PGRAMVDIIL LLSDKDPPKL 

       190        200        210        220        230        240 
KDYLPTVGAL KHLREWYSAK ITIAGNHCEI NCQKIAEYLS ANVVSLEDLR NVIDSKELWR 

       250        260        270        280        290        300 
GKIQIWERKF GFEISFPEFC LKGVTLKNFS TSNLNTDFLA KKIIPSKDKN ILPKVFHYYG 

       310        320        330        340        350        360 
PALEFVQMIK LSDLPSCYMS DIEFELGLTN STKQNSVLLL EQISSLCSKV GALFVLPCTI 

       370        380        390        400        410        420 
SNILIPPPNQ LSSRKWKEYI AKKPKTISVP DVEVKGECSS YYLLLQGNGN RRCKATLIHS 

       430        440        450        460        470        480 
ANQINGSFAL NLIHGKMKTK TEEAKLSFPF DLLSLPHFSG EQIVQREKQL ANVQVLALEE 

       490        500        510        520        530        540 
CLKRRKLAKQ PETVSVAELK SLLVLTRKHF LDYFDAVIPK MILRKMDKIK TFNILNDFSP 

       550        560        570        580        590        600 
VEPNSSSLME TNPLEWPERH VLQNLETFEK TKQKMRTGSL PHSSEQLLGH KEGPRDSITL 

       610        620        630        640        650        660 
LDAKELLKYF TSDGLPIGDL QPLPIQKGEK TFVLTPELSP GKLQVLPFEK ASVCHYHGIE 

       670        680        690        700        710        720 
YCLDDRKALE RDGGFSELQS RLIRYETQTT CTRESFPVPT VLSPLPSPVV SSDPGSVPDG 

       730        740        750        760        770        780 
EVLQNELRTE VSRLKRRSKD LNCLYPRKRL VKSESSESLL SQTTGNSNHY HHHVTSRKPQ 

       790        800        810        820        830        840 
TERSLPVTCP LVPIPSCETP KLATKTSSGQ KSMHESKTSR QIKESRSQKH TRILKEVVTE 

       850        860        870        880        890        900 
TLKKHSITET HECFTACSQR LFEISKFYLK DLKTSRGLFE EMKKTANNNA VQVIDWVLEK 


TSKK 

« Hide

References

« Hide 'large scale' references
[1]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-141.
Tissue: Embryo.
[4]"Regulation of p53 and MDM2 activity by MTBP."
Brady M., Vlatkovic N., Boyd M.T.
Mol. Cell. Biol. 25:545-553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH471060 Genomic DNA. Translation: EAW92006.1.
CH471060 Genomic DNA. Translation: EAW92007.1. Sequence problems.
BC013136 mRNA. Translation: AAH13136.1.
AK022122 mRNA. Translation: BAB13965.1. Sequence problems.
CCDSCCDS6333.1.
RefSeqNP_071328.2. NM_022045.4.
UniGeneHs.657656.

3D structure databases

ProteinModelPortalQ96DY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117988. 3 interactions.
IntActQ96DY7. 1 interaction.
STRING9606.ENSP00000303398.

PTM databases

PhosphoSiteQ96DY7.

Polymorphism databases

DMDM74731509.

Proteomic databases

MaxQBQ96DY7.
PaxDbQ96DY7.
PRIDEQ96DY7.

Protocols and materials databases

DNASU27085.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305949; ENSP00000303398; ENSG00000172167.
GeneID27085.
KEGGhsa:27085.
UCSCuc003ypc.2. human.

Organism-specific databases

CTD27085.
GeneCardsGC08P121526.
HGNCHGNC:7417. MTBP.
HPAHPA025694.
MIM605927. gene.
neXtProtNX_Q96DY7.
PharmGKBPA31224.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45076.
HOGENOMHOG000113675.
HOVERGENHBG108152.
InParanoidQ96DY7.
OMAFPEFCLK.
OrthoDBEOG7K0ZBM.
PhylomeDBQ96DY7.
TreeFamTF331503.

Gene expression databases

ArrayExpressQ96DY7.
BgeeQ96DY7.
CleanExHS_MTBP.
GenevestigatorQ96DY7.

Family and domain databases

InterProIPR029418. MTBP_C.
IPR029420. MTBP_central.
IPR029421. MTBP_N.
[Graphical view]
PfamPF14920. MTBP_C. 1 hit.
PF14919. MTBP_mid. 1 hit.
PF14918. MTBP_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi27085.
NextBio49689.
PROQ96DY7.
SOURCESearch...

Entry information

Entry nameMTBP_HUMAN
AccessionPrimary (citable) accession number: Q96DY7
Secondary accession number(s): Q9HA89
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM