ZBT7A_HUMAN - dbPTM
ZBT7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT7A_HUMAN
UniProt AC O95365
Protein Name Zinc finger and BTB domain-containing protein 7A
Gene Name ZBTB7A
Organism Homo sapiens (Human).
Sequence Length 584
Subcellular Localization Nucleus.
Protein Description Plays a key role in the instruction of early lymphoid progenitors to develop into B lineage by repressing T-cell instructive Notch signals (By similarity). Specifically represses the transcription of the CDKN2A gene. Efficiently abrogates E2F1-dependent CDKN2A transactivation/de-repression. Binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' (By similarity)..
Protein Sequence MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLDRQILAADAGADAGQLDLVDQIDQRNLLRAKEYLEFFQSNPMNSLPPAAAAAAASFPWSAFGASDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPAERPPTGDGDEGDSNPGLWPERDEDAPTGGLFPPPVAPPAATQNGHYGRGGEEEAASLSEAAPEPGDSPGFLSGAAEGEDGDGPDVDGLAASTLLQQMMSSVGRAGAAAGDSDEESRADDKGVMDYYLKYFSGAHDGDVYPAWSQKVEKKIRAKAFQKCPICEKVIQGAGKLPRHIRTHTGEKPYECNICKVRFTRQDKLKVHMRKHTGEKPYLCQQCGAAFAHNYDLKNHMRVHTGLRPYQCDSCCKTFVRSDHLHRHLKKDGCNGVPSRRGRKPRVRGGAPDPSPGATATPGAPAQPSSPDARRNGQEKHFKDEDEDEDVASPDGLGRLNVAGAGGGGDSGGGPGAATDGNFTAGLA
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
60AcetylationAACSQYFKKLFTSGA
HHHHHHHHHHHCCCC		43.5726051181
61SumoylationACSQYFKKLFTSGAV
HHHHHHHHHHCCCCE		38.65-
61SumoylationACSQYFKKLFTSGAV
HHHHHHHHHHCCCCE		38.65-
191PhosphorylationPWSAFGASDDDLDAT
CHHHCCCCHHCHHHH		41.7927251275
239PhosphorylationGDGDEGDSNPGLWPE
CCCCCCCCCCCCCCC		56.6426074081
284PhosphorylationEEEAASLSEAAPEPG
HHHHHHHHHHCCCCC		23.7727362937
293PhosphorylationAAPEPGDSPGFLSGA
HCCCCCCCCCCCCCC		32.6027362937
298PhosphorylationGDSPGFLSGAAEGED
CCCCCCCCCCCCCCC		24.9128348404
337PhosphorylationAGAAAGDSDEESRAD
HHHHCCCCCHHHHHC		46.1029255136
341PhosphorylationAGDSDEESRADDKGV
CCCCCHHHHHCCCCH		30.6229255136
351PhosphorylationDDKGVMDYYLKYFSG
CCCCHHHHHHHHHCC		7.8123403867
352PhosphorylationDKGVMDYYLKYFSGA
CCCHHHHHHHHHCCC		7.7723403867
369PhosphorylationGDVYPAWSQKVEKKI
CCCCHHHHHHHHHHH		23.4128555341
371AcetylationVYPAWSQKVEKKIRA
CCHHHHHHHHHHHHH		47.0126051181
371UbiquitinationVYPAWSQKVEKKIRA
CCHHHHHHHHHHHHH		47.0129967540
374AcetylationAWSQKVEKKIRAKAF
HHHHHHHHHHHHHHH		57.3926051181
379UbiquitinationVEKKIRAKAFQKCPI
HHHHHHHHHHHHCCH		39.6327667366
389AcetylationQKCPICEKVIQGAGK
HHCCHHHHHHCCCCC		39.9825953088
396UbiquitinationKVIQGAGKLPRHIRT
HHHCCCCCCCCCCCC		55.5829967540
396AcetylationKVIQGAGKLPRHIRT
HHHCCCCCCCCCCCC		55.5825953088
403PhosphorylationKLPRHIRTHTGEKPY
CCCCCCCCCCCCCCE		24.1628450419
405PhosphorylationPRHIRTHTGEKPYEC
CCCCCCCCCCCCEEC		46.5628450419
410PhosphorylationTHTGEKPYECNICKV
CCCCCCCEECCEEEE		44.1528152594
429UbiquitinationQDKLKVHMRKHTGEK
CCCHHHEEECCCCCC		7.3627667366
433PhosphorylationKVHMRKHTGEKPYLC
HHEEECCCCCCCCHH		50.5023532336
436SumoylationMRKHTGEKPYLCQQC
EECCCCCCCCHHHHC		40.0628112733
438PhosphorylationKHTGEKPYLCQQCGA
CCCCCCCCHHHHCCC		31.0429214152
461PhosphorylationKNHMRVHTGLRPYQC
CCCCEECCCCCCCCC		34.7525159151
466PhosphorylationVHTGLRPYQCDSCCK
ECCCCCCCCCCHHHH		18.4928555341
478PhosphorylationCCKTFVRSDHLHRHL
HHHHHHCHHHHHHHH		24.8728555341
495PhosphorylationDGCNGVPSRRGRKPR
HCCCCCCCCCCCCCC		32.0024505115
511PhosphorylationRGGAPDPSPGATATP
CCCCCCCCCCCCCCC		43.2630278072
515PhosphorylationPDPSPGATATPGAPA
CCCCCCCCCCCCCCC		36.6630278072
517PhosphorylationPSPGATATPGAPAQP
CCCCCCCCCCCCCCC		20.2123927012
525PhosphorylationPGAPAQPSSPDARRN
CCCCCCCCCCCHHHC		42.2829255136
526PhosphorylationGAPAQPSSPDARRNG
CCCCCCCCCCHHHCC		33.2229255136
536AcetylationARRNGQEKHFKDEDE
HHHCCCCCCCCCCCC		46.5925953088
539AcetylationNGQEKHFKDEDEDED
CCCCCCCCCCCCCCC		60.9926051181
539SumoylationNGQEKHFKDEDEDED
CCCCCCCCCCCCCCC		60.9928112733
539SumoylationNGQEKHFKDEDEDED
CCCCCCCCCCCCCCC		60.99-
549PhosphorylationDEDEDVASPDGLGRL
CCCCCCCCCCCCCCC		24.3029255136
567PhosphorylationGAGGGGDSGGGPGAA
CCCCCCCCCCCCCCC		42.4825159151
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 ZBT7A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBT7A_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 ZBT7A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT7A_HUMANZBTB7Aphysical
9973611
BCL6_HUMANBCL6physical
9927193
SP1_MOUSESp1physical
12004059
P53_HUMANTP53physical
19244234
HDAC1_HUMANHDAC1physical
19244234
HDAC2_HUMANHDAC2physical
19244234
HDAC3_HUMANHDAC3physical
19244234
SIR1_HUMANSIRT1physical
19244234
NCOR1_HUMANNCOR1physical
19244234
NCOR2_HUMANNCOR2physical
19244234
SIN3A_HUMANSIN3Aphysical
19244234
ZBT7A_HUMANZBTB7Aphysical
17189472
RB_HUMANRB1physical
18801742
BCOR_HUMANBCORphysical
18801742
SP1_HUMANSP1physical
18368381
EF1A1_HUMANEEF1A1physical
19471103
SRBP1_HUMANSREBF1physical
18682402
TF65_HUMANRELAphysical
15917220
IKBB_HUMANNFKBIBphysical
15917220
IKBA_HUMANNFKBIAphysical
15917220
PKCB1_HUMANZMYND8physical
21988832
TZAP_HUMANZBTB48physical
24382891
HOMEZ_HUMANHOMEZphysical
25416956
KHDR1_HUMANKHDRBS1physical
24514149
ETS1_HUMANETS1physical
24857950
P53_HUMANTP53physical
24857950
SMAD4_HUMANSMAD4physical
25514493
HDAC1_HUMANHDAC1physical
25514493
ZBT7A_HUMANZBTB7Aphysical
21804610
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 ZBT7A_HUMAN

loading...

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-511; SER-525 ANDSER-549, 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-525 AND SER-526, ANDMASS SPECTROMETRY.
"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-526 AND SER-549, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-526 ANDSER-549, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory