ZBT11_HUMAN - dbPTM
ZBT11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT11_HUMAN
UniProt AC O95625
Protein Name Zinc finger and BTB domain-containing protein 11
Gene Name ZBTB11
Organism Homo sapiens (Human).
Sequence Length 1053
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MSSEESYRAILRYLTNEREPYAPGTEGNVKRKIRKAAACYVVRGGTLYYQRRQRHRKTFAELEVVLQPERRRDLIEAAHLGPGGTHHTRHQTWHYLSKTYWWRGILKQVKDYIKQCSKCQEKLDRSRPISDVSEMLEELGLDLESGEESNESEDDLSNFTSSPTTASKPAKKKPVSKHELVFVDTKGVVKRSSPKHCQAVLKQLNEQRLSNQFCDVTLLIEGEEYKAHKSVLSANSEYFRDLFIEKGAVSSHEAVVDLSGFCKASFLPLLEFAYTSVLSFDFCSMADVAILARHLFMSEVLEICESVHKLMEEKQLTVYKKGEVQTVASTQDLRVQNGGTAPPVASSEGTTTSLPTELGDCEIVLLVNGELPEAEQNGEVGRQPEPQVSSEAESALSSVGCIADSHPEMESVDLITKNNQTELETSNNRENNTVSNIHPKLSKENVISSSPEDSGMGNDISAEDICAEDIPKHRQKVDQPLKDQENLVASTAKTDFGPDDDTYRSRLRQRSVNEGAYIRLHKGMEKKLQKRKAVPKSAVQQVAQKLVQRGKKMKQPKRDAKENTEEASHKCGECGMVFQRRYALIMHKLKHERARDYKCPLCKKQFQYSASLRAHLIRHTRKDAPSSSSSNSTSNEASGTSSEKGRTKREFICSICGRTLPKLYSLRIHMLKHTGVKPHACQVCGKTFIYKHGLKLHQSLHQSQKQFQCELCVKSFVTKRSLQEHMSIHTGESKYLCSVCGKSFHRGSGLSKHFKKHQPKPEVRGYHCTQCEKSFFEARDLRQHMNKHLGVKPFQCQFCDKCYSWKKDWYSHVKSHSVTEPYRCNICGKEFYEKALFRRHVKKATHGKKGRAKQNLERVCEKCGRKFTQLREYRRHMNNHEGVKPFECLTCGVAWADARSLKRHVRTHTGERPYVCPVCSEAYIDARTLRKHMTKFHRDYVPCKIMLEKDTLQFHNQGTQVAHAVSILTAGMQEQESSGPQELETVVVTGETMEALEAVAATEEYPSVSTLSDQSIMQVVNYVLAQQQGQKLSEVAEAIQTVKVEVAHISGGE
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
13PhosphorylationSYRAILRYLTNEREP
HHHHHHHHHHCCCCC
17.9027251275
15PhosphorylationRAILRYLTNEREPYA
HHHHHHHHCCCCCCC
26.5427251275
30UbiquitinationPGTEGNVKRKIRKAA
CCCCCCHHHHHHHHH
52.5621906983
98AcetylationQTWHYLSKTYWWRGI
HHHHHHCHHHHHHHH
42.9312655513
110UbiquitinationRGILKQVKDYIKQCS
HHHHHHHHHHHHHHH
42.17-
114UbiquitinationKQVKDYIKQCSKCQE
HHHHHHHHHHHHHHH
38.74-
126PhosphorylationCQEKLDRSRPISDVS
HHHHHHCCCCCCHHH
41.9217081983
130PhosphorylationLDRSRPISDVSEMLE
HHCCCCCCHHHHHHH
34.3417081983
133PhosphorylationSRPISDVSEMLEELG
CCCCCHHHHHHHHCC
23.4417081983
145PhosphorylationELGLDLESGEESNES
HCCCCCCCCCCCCCC
59.8222817900
149PhosphorylationDLESGEESNESEDDL
CCCCCCCCCCCCCHH
41.4122817900
152PhosphorylationSGEESNESEDDLSNF
CCCCCCCCCCHHCCC
51.0422817900
157PhosphorylationNESEDDLSNFTSSPT
CCCCCHHCCCCCCCC
36.5717081983
160PhosphorylationEDDLSNFTSSPTTAS
CCHHCCCCCCCCCCC
32.3317081983
161PhosphorylationDDLSNFTSSPTTASK
CHHCCCCCCCCCCCC
30.1317081983
162PhosphorylationDLSNFTSSPTTASKP
HHCCCCCCCCCCCCC
24.1717081983
165PhosphorylationNFTSSPTTASKPAKK
CCCCCCCCCCCCCCC
32.1117081983
167PhosphorylationTSSPTTASKPAKKKP
CCCCCCCCCCCCCCC
36.7617081983
186UbiquitinationELVFVDTKGVVKRSS
CEEEECCCCCCCCCC
45.29-
186SumoylationELVFVDTKGVVKRSS
CEEEECCCCCCCCCC
45.29-
186SumoylationELVFVDTKGVVKRSS
CEEEECCCCCCCCCC
45.29-
192PhosphorylationTKGVVKRSSPKHCQA
CCCCCCCCCHHHHHH
45.32-
193PhosphorylationKGVVKRSSPKHCQAV
CCCCCCCCHHHHHHH
41.84-
195UbiquitinationVVKRSSPKHCQAVLK
CCCCCCHHHHHHHHH
59.98-
202UbiquitinationKHCQAVLKQLNEQRL
HHHHHHHHHHHHHHH
46.25-
229UbiquitinationGEEYKAHKSVLSANS
CCHHHHCHHHHHCCC
47.31-
230PhosphorylationEEYKAHKSVLSANSE
CHHHHCHHHHHCCCH
20.5821406692
233PhosphorylationKAHKSVLSANSEYFR
HHCHHHHHCCCHHHH
24.2121406692
236PhosphorylationKSVLSANSEYFRDLF
HHHHHCCCHHHHHHH
33.1321406692
238PhosphorylationVLSANSEYFRDLFIE
HHHCCCHHHHHHHHH
12.0721406692
246UbiquitinationFRDLFIEKGAVSSHE
HHHHHHHCCCCCCCC
47.56-
314UbiquitinationVHKLMEEKQLTVYKK
HHHHHHHCCEEEEEC
36.98-
317PhosphorylationLMEEKQLTVYKKGEV
HHHHCCEEEEECCEE
21.2123532336
319PhosphorylationEEKQLTVYKKGEVQT
HHCCEEEEECCEEEE
11.1828102081
321UbiquitinationKQLTVYKKGEVQTVA
CCEEEEECCEEEEEE
42.49-
329PhosphorylationGEVQTVASTQDLRVQ
CEEEEEEECCCEEEC
23.43-
334MethylationVASTQDLRVQNGGTA
EEECCCEEECCCCCC
35.9424411709
334DimethylationVASTQDLRVQNGGTA
EEECCCEEECCCCCC
35.94-
426PhosphorylationNQTELETSNNRENNT
CCCEEECCCCCCCCC
23.8029214152
433PhosphorylationSNNRENNTVSNIHPK
CCCCCCCCCCCCCHH
36.5728555341
442PhosphorylationSNIHPKLSKENVISS
CCCCHHCCCCCCCCC
44.0130576142
448PhosphorylationLSKENVISSSPEDSG
CCCCCCCCCCCCCCC
22.0828102081
449PhosphorylationSKENVISSSPEDSGM
CCCCCCCCCCCCCCC
38.5025159151
450PhosphorylationKENVISSSPEDSGMG
CCCCCCCCCCCCCCC
26.0528102081
454PhosphorylationISSSPEDSGMGNDIS
CCCCCCCCCCCCCCC
29.0823663014
461PhosphorylationSGMGNDISAEDICAE
CCCCCCCCHHHHCHH
28.5923663014
482AcetylationQKVDQPLKDQENLVA
HHCCCCCCCCHHHHH
65.1426051181
482UbiquitinationQKVDQPLKDQENLVA
HHCCCCCCCCHHHHH
65.14-
493UbiquitinationNLVASTAKTDFGPDD
HHHHHHCCCCCCCCC
49.03-
511PhosphorylationRSRLRQRSVNEGAYI
HHHHHHCCCCCCHHH
22.4325159151
517PhosphorylationRSVNEGAYIRLHKGM
CCCCCCHHHHHCCHH
9.4617360941
537PhosphorylationKRKAVPKSAVQQVAQ
HCCCCCHHHHHHHHH
27.83-
545AcetylationAVQQVAQKLVQRGKK
HHHHHHHHHHHCCHH
40.6725953088
609PhosphorylationCKKQFQYSASLRAHL
HHHHHCCCHHHHHHH
10.7024719451
611PhosphorylationKQFQYSASLRAHLIR
HHHCCCHHHHHHHHH
16.6724719451
620O-linked_GlycosylationRAHLIRHTRKDAPSS
HHHHHHHCCCCCCCC
29.5730620550
626PhosphorylationHTRKDAPSSSSSNST
HCCCCCCCCCCCCCC
44.5730576142
627PhosphorylationTRKDAPSSSSSNSTS
CCCCCCCCCCCCCCC
32.9330576142
629PhosphorylationKDAPSSSSSNSTSNE
CCCCCCCCCCCCCCC
35.1730576142
630PhosphorylationDAPSSSSSNSTSNEA
CCCCCCCCCCCCCCC
36.4330576142
632PhosphorylationPSSSSSNSTSNEASG
CCCCCCCCCCCCCCC
34.8530576142
633PhosphorylationSSSSSNSTSNEASGT
CCCCCCCCCCCCCCC
39.5630576142
640PhosphorylationTSNEASGTSSEKGRT
CCCCCCCCCCCCCCC
26.9530576142
642PhosphorylationNEASGTSSEKGRTKR
CCCCCCCCCCCCCHH
43.0730576142
665PhosphorylationRTLPKLYSLRIHMLK
CCHHHHHHHHHHHHH
22.9324719451
674PhosphorylationRIHMLKHTGVKPHAC
HHHHHHHCCCCHHHC
41.92-
687PhosphorylationACQVCGKTFIYKHGL
HCCCCCCCHHHHHCH
10.6829083192
690PhosphorylationVCGKTFIYKHGLKLH
CCCCCHHHHHCHHHH
7.8529083192
699PhosphorylationHGLKLHQSLHQSQKQ
HCHHHHHHHHHHHHH
19.6429083192
703PhosphorylationLHQSLHQSQKQFQCE
HHHHHHHHHHHHCHH
28.7029083192
721PhosphorylationKSFVTKRSLQEHMSI
HHHHCHHHHHHHHCC
35.6425137130
727PhosphorylationRSLQEHMSIHTGESK
HHHHHHHCCCCCCCH
17.0825137130
730PhosphorylationQEHMSIHTGESKYLC
HHHHCCCCCCCHHHH
40.7629978859
733PhosphorylationMSIHTGESKYLCSVC
HCCCCCCCHHHHCCC
28.1329978859
743PhosphorylationLCSVCGKSFHRGSGL
HHCCCCCCCCCCCCH
16.1525137130
746MethylationVCGKSFHRGSGLSKH
CCCCCCCCCCCHHHH
38.67115920301
748O-linked_GlycosylationGKSFHRGSGLSKHFK
CCCCCCCCCHHHHHH
36.2030620550
751O-linked_GlycosylationFHRGSGLSKHFKKHQ
CCCCCCHHHHHHHCC
27.8430620550
773UbiquitinationYHCTQCEKSFFEARD
CCCCHHCHHHHHHHH
61.25-
792UbiquitinationMNKHLGVKPFQCQFC
HHHHCCCCCEECCCC
38.01-
792AcetylationMNKHLGVKPFQCQFC
HHHHCCCCCEECCCC
38.0126051181
815PhosphorylationDWYSHVKSHSVTEPY
HHHHCCHHCCCCCCE
21.6529396449
817PhosphorylationYSHVKSHSVTEPYRC
HHCCHHCCCCCCEEC
37.5129496963
819PhosphorylationHVKSHSVTEPYRCNI
CCHHCCCCCCEECCC
33.9722817900
834UbiquitinationCGKEFYEKALFRRHV
CCHHHHHHHHHHHHH
38.72-
909PhosphorylationKRHVRTHTGERPYVC
HHHHHHCCCCCCEEC
39.8721857030
944UbiquitinationHRDYVPCKIMLEKDT
CCCCCCEEEEEECCC
25.69-
1043UbiquitinationAEAIQTVKVEVAHIS
HHHHHHCEEEEEECC
35.74-
1043SumoylationAEAIQTVKVEVAHIS
HHHHHHCEEEEEECC
35.7428112733
1050PhosphorylationKVEVAHISGGE----
EEEEEECCCCC----
30.7723401153

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
511SPhosphorylationKinaseCHEK1O14757
GPS
537SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBT11_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 ZBT11_HUMAN !!

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

Oops, there are no PPI records of ZBT11_HUMAN !!

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 ZBT11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1050, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1050, AND MASSSPECTROMETRY.

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