MTBP_HUMAN - dbPTM
MTBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTBP_HUMAN
UniProt AC Q96DY7
Protein Name Mdm2-binding protein
Gene Name MTBP
Organism Homo sapiens (Human).
Sequence Length 904
Subcellular Localization
Protein Description 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..
Protein Sequence MDRYLLLVIWGEGKFPSAASREAEHGPEVSSGEGTENQPDFTAANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWFFAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPAPGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEINCQKIAEYLSANVVSLEDLRNVIDSKELWRGKIQIWERKFGFEISFPEFCLKGVTLKNFSTSNLNTDFLAKKIIPSKDKNILPKVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLTNSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLSSRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFDLLSLPHFSGEQIVQREKQLANVQVLALEECLKRRKLAKQPETVSVAELKSLLVLTRKHFLDYFDAVIPKMILRKMDKIKTFNILNDFSPVEPNSSSLMETNPLEWPERHVLQNLETFEKTKQKMRTGSLPHSSEQLLGHKEGPRDSITLLDAKELLKYFTSDGLPIGDLQPLPIQKGEKTFVLTPELSPGKLQVLPFEKASVCHYHGIEYCLDDRKALERDGGFSELQSRLIRYETQTTCTRESFPVPTVLSPLPSPVVSSDPGSVPDGEVLQNELRTEVSRLKRRSKDLNCLYPRKRLVKSESSESLLSQTTGNSNHYHHHVTSRKPQTERSLPVTCPLVPIPSCETPKLATKTSSGQKSMHESKTSRQIKESRSQKHTRILKEVVTETLKKHSITETHECFTACSQRLFEISKFYLKDLKTSRGLFEEMKKTANNNAVQVIDWVLEKTSKK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
51UbiquitinationANVYHLLKRSISASI
HHHHHHHHHHHHCCC
50.9229967540
51UbiquitinationANVYHLLKRSISASI
HHHHHHHHHHHHCCC
50.92-
137PhosphorylationEDSNSRESLSLADLY
CCCCCCHHCCHHHHH
23.3425072903
139PhosphorylationSNSRESLSLADLYEE
CCCCHHCCHHHHHHH
30.6925072903
144PhosphorylationSLSLADLYEEAAENL
HCCHHHHHHHHHHHH
16.5725072903
155PhosphorylationAENLHQLSDKLPAPG
HHHHHHHHHCCCCCC
26.5725072903
181UbiquitinationDKDPPKLKDYLPTVG
CCCCHHHHHHHCHHH
50.9129967540
225PhosphorylationYLSANVVSLEDLRNV
HHHCCCCCHHHHHHC
23.0422167270
236UbiquitinationLRNVIDSKELWRGKI
HHHCCCCHHHHCCCE
53.75-
236UbiquitinationLRNVIDSKELWRGKI
HHHCCCCHHHHCCCE
53.7529967540
242UbiquitinationSKELWRGKIQIWERK
CHHHHCCCEEEEHHH
23.90-
242UbiquitinationSKELWRGKIQIWERK
CHHHHCCCEEEEHHH
23.90-
267UbiquitinationCLKGVTLKNFSTSNL
HCCCCEECCCCCCCC
46.73-
267UbiquitinationCLKGVTLKNFSTSNL
HCCCCEECCCCCCCC
46.7329967540
281UbiquitinationLNTDFLAKKIIPSKD
CCHHHHHHHHCCCCC
46.8029967540
281UbiquitinationLNTDFLAKKIIPSKD
CCHHHHHHHHCCCCC
46.80-
286PhosphorylationLAKKIIPSKDKNILP
HHHHHCCCCCCCCCC
42.9824719451
379PhosphorylationSSRKWKEYIAKKPKT
CCHHHHHHHHCCCCE
11.49-
386PhosphorylationYIAKKPKTISVPDVE
HHHCCCCEEECCCEE
27.3228796482
388PhosphorylationAKKPKTISVPDVEVK
HCCCCEEECCCEEEE
32.5928796482
468UbiquitinationEQIVQREKQLANVQV
HHHHHHHHHHHHHHH
53.4529967540
483UbiquitinationLALEECLKRRKLAKQ
HHHHHHHHHHHHHCC
62.91-
500UbiquitinationTVSVAELKSLLVLTR
CCCHHHHHHHHHHHH
30.48-
531PhosphorylationRKMDKIKTFNILNDF
HCHHHCCCEECCCCC
25.9528450419
539PhosphorylationFNILNDFSPVEPNSS
EECCCCCCCCCCCCC
30.7928464451
545PhosphorylationFSPVEPNSSSLMETN
CCCCCCCCCCCCCCC
31.8328176443
546PhosphorylationSPVEPNSSSLMETNP
CCCCCCCCCCCCCCC
33.8528176443
547PhosphorylationPVEPNSSSLMETNPL
CCCCCCCCCCCCCCC
31.4028176443
551PhosphorylationNSSSLMETNPLEWPE
CCCCCCCCCCCCCHH
28.3328176443
570UbiquitinationQNLETFEKTKQKMRT
HHHHHHHHHHHHHHH
57.7521906983
570 (in isoform 1)Ubiquitination-57.7521890473
572UbiquitinationLETFEKTKQKMRTGS
HHHHHHHHHHHHHCC
60.0122817900
574UbiquitinationTFEKTKQKMRTGSLP
HHHHHHHHHHHCCCC
31.7222817900
577PhosphorylationKTKQKMRTGSLPHSS
HHHHHHHHCCCCCCH
27.85-
579PhosphorylationKQKMRTGSLPHSSEQ
HHHHHHCCCCCCHHH
37.8128555341
591UbiquitinationSEQLLGHKEGPRDSI
HHHHCCCCCCCCCCE
63.6721906983
591 (in isoform 1)Ubiquitination-63.6721890473
597PhosphorylationHKEGPRDSITLLDAK
CCCCCCCCEEEECHH
20.8225159151
599PhosphorylationEGPRDSITLLDAKEL
CCCCCCEEEECHHHH
25.8129396449
604 (in isoform 1)Ubiquitination-48.8621890473
604UbiquitinationSITLLDAKELLKYFT
CEEEECHHHHHHHHC
48.8621906983
608 (in isoform 1)Ubiquitination-51.4421890473
608UbiquitinationLDAKELLKYFTSDGL
ECHHHHHHHHCCCCC
51.4421906983
627 (in isoform 1)Ubiquitination-70.5221890473
627UbiquitinationLQPLPIQKGEKTFVL
CEECCCCCCCEEEEE
70.5221906983
630 (in isoform 1)Ubiquitination-56.8021890473
630UbiquitinationLPIQKGEKTFVLTPE
CCCCCCCEEEEECCC
56.8021890473
630UbiquitinationLPIQKGEKTFVLTPE
CCCCCCCEEEEECCC
56.8022817900
631PhosphorylationPIQKGEKTFVLTPEL
CCCCCCEEEEECCCC
18.0524732914
635PhosphorylationGEKTFVLTPELSPGK
CCEEEEECCCCCCCC
14.9330266825
639PhosphorylationFVLTPELSPGKLQVL
EEECCCCCCCCEEEE
29.9119664994
642 (in isoform 1)Ubiquitination-38.8521890473
642UbiquitinationTPELSPGKLQVLPFE
CCCCCCCCEEEEECC
38.8522817900
687PhosphorylationSRLIRYETQTTCTRE
HHHHHHCCCCCCCCC
23.45-
695PhosphorylationQTTCTRESFPVPTVL
CCCCCCCCCCCCEEE
31.4024400094
700PhosphorylationRESFPVPTVLSPLPS
CCCCCCCEEECCCCC
34.0224400094
703PhosphorylationFPVPTVLSPLPSPVV
CCCCEEECCCCCCCC
21.7622817900
707PhosphorylationTVLSPLPSPVVSSDP
EEECCCCCCCCCCCC
37.7014702039
711PhosphorylationPLPSPVVSSDPGSVP
CCCCCCCCCCCCCCC
29.2928634120
716PhosphorylationVVSSDPGSVPDGEVL
CCCCCCCCCCCCHHH
35.5528634120
738PhosphorylationVSRLKRRSKDLNCLY
HHHHHHHHHCCCCCC
34.2624719451
739MethylationSRLKRRSKDLNCLYP
HHHHHHHHCCCCCCC
65.51115973331
752SumoylationYPRKRLVKSESSESL
CCCCHHCCCCCHHHH
53.77-
752SumoylationYPRKRLVKSESSESL
CCCCHHCCCCCHHHH
53.77-
753PhosphorylationPRKRLVKSESSESLL
CCCHHCCCCCHHHHH
34.9221406692
755PhosphorylationKRLVKSESSESLLSQ
CHHCCCCCHHHHHHC
46.6330576142
756PhosphorylationRLVKSESSESLLSQT
HHCCCCCHHHHHHCC
27.4430576142
758PhosphorylationVKSESSESLLSQTTG
CCCCCHHHHHHCCCC
36.2430576142
761PhosphorylationESSESLLSQTTGNSN
CCHHHHHHCCCCCCC
30.6721406692
763PhosphorylationSESLLSQTTGNSNHY
HHHHHHCCCCCCCCC
33.0421406692
764PhosphorylationESLLSQTTGNSNHYH
HHHHHCCCCCCCCCC
27.0821406692
767PhosphorylationLSQTTGNSNHYHHHV
HHCCCCCCCCCCEEC
26.7421406692
770PhosphorylationTTGNSNHYHHHVTSR
CCCCCCCCCEECCCC
13.7021406692
775PhosphorylationNHYHHHVTSRKPQTE
CCCCEECCCCCCCCC
20.6123312004
776PhosphorylationHYHHHVTSRKPQTER
CCCEECCCCCCCCCC
36.9021406692
784PhosphorylationRKPQTERSLPVTCPL
CCCCCCCCCCCCCCE
30.6923312004
788PhosphorylationTERSLPVTCPLVPIP
CCCCCCCCCCEEECC
13.3823312004
796PhosphorylationCPLVPIPSCETPKLA
CCEEECCCCCCCCCC
25.8830576142
799PhosphorylationVPIPSCETPKLATKT
EECCCCCCCCCCEEC
30.0125850435
804PhosphorylationCETPKLATKTSSGQK
CCCCCCCEECCCCCH
45.3423312004
812PhosphorylationKTSSGQKSMHESKTS
ECCCCCHHHCCCHHH
19.9330576142
844UbiquitinationVVTETLKKHSITETH
HHHHHHHHCCCCCHH
45.7729967540
846PhosphorylationTETLKKHSITETHEC
HHHHHHCCCCCHHHH
39.83-
855PhosphorylationTETHECFTACSQRLF
CCHHHHHHHHHHHHH
38.11-
866UbiquitinationQRLFEISKFYLKDLK
HHHHHHHHHHHHHHH
43.63-
883UbiquitinationRGLFEEMKKTANNNA
CCHHHHHHHHCCCCH
50.6929967540
884UbiquitinationGLFEEMKKTANNNAV
CHHHHHHHHCCCCHH
52.11-
904UbiquitinationVLEKTSKK-------
HHHHHCCC-------
66.40-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MTBP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTBP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MTBP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_HUMANMDM2genetic
10906133

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTBP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639; SER-703 ANDSER-707, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.

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