ZBT20_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZBT20_HUMAN
• UniProt AC: Q9HC78
• Protein Name: Zinc finger and BTB domain-containing protein 20
• Gene Name: ZBTB20
• Organism: Homo sapiens (Human).
• Sequence Length: 741
• Subcellular Localization: Nucleus .
• Protein Description: May be a transcription factor that may be involved in hematopoiesis, oncogenesis, and immune responses. [PubMed: 11352661 Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (By similarity]
• Protein Sequence: MLERKKPKTAENQKASEENEITQPGGSSAKPGLPCLNFEAVLSPDPALIHSTHSLTNSHAHTGSSDCDISCKGMTERIHSINLHNFSNSVLETLNEQRNRGHFCDVTVRIHGSMLRAHRCVLAAGSPFFQDKLLLGYSDIEIPSVVSVQSVQKLIDFMYSGVLRVSQSEALQILTAASILQIKTVIDECTRIVSQNVGDVFPGIQDSGQDTPRGTPESGTSGQSSDTESGYLQSHPQHSVDRIYSALYACSMQNGSGERSFYSGAVVSHHETALGLPRDHHMEDPSWITRIHERSQQMERYLSTTPETTHCRKQPRPVRIQTLVGNIHIKQEMEDDYDYYGQQRVQILERNESEECTEDTDQAEGTESEPKGESFDSGVSSSIGTEPDSVEQQFGPGAARDSQAEPTQPEQAAEAPAEGGPQTNQLETGASSPERSNEVEMDSTVITVSNSSDKSVLQQPSVNTSIGQPLPSTQLYLRQTETLTSNLRMPLTLTSNTQVIGTAGNTYLPALFTTQPAGSGPKPFLFSLPQPLAGQQTQFVTVSQPGLSTFTAQLPAPQPLASSAGHSTASGQGEKKPYECTLCNKTFTAKQNYVKHMFVHTGEKPHQCSICWRSFSLKDYLIKHMVTHTGVRAYQCSICNKRFTQKSSLNVHMRLHRGEKSYECYICKKKFSHKTLLERHVALHSASNGTPPAGTPPGARAGPPGVVACTEGTTYVCSVCPAKFDQIEQFNDHMRMHVSDG

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
194	Phosphorylation	DECTRIVSQNVGDVF HHHHHHHHCCCCCCC	17.42	30266825
207	Phosphorylation	VFPGIQDSGQDTPRG CCCCCCCCCCCCCCC	23.21	30266825
211	Phosphorylation	IQDSGQDTPRGTPES CCCCCCCCCCCCCCC	13.65	26657352
215	Phosphorylation	GQDTPRGTPESGTSG CCCCCCCCCCCCCCC	25.76	23186163
218	Phosphorylation	TPRGTPESGTSGQSS CCCCCCCCCCCCCCC	48.88	23186163
220	Phosphorylation	RGTPESGTSGQSSDT CCCCCCCCCCCCCCC	38.68	29116813
221	Phosphorylation	GTPESGTSGQSSDTE CCCCCCCCCCCCCCC	38.06	23186163
224	Phosphorylation	ESGTSGQSSDTESGY CCCCCCCCCCCCCCC	33.43	29116813
225	Phosphorylation	SGTSGQSSDTESGYL CCCCCCCCCCCCCCC	40.44	29116813
227	Phosphorylation	TSGQSSDTESGYLQS CCCCCCCCCCCCCCC	33.72	29116813
229	Phosphorylation	GQSSDTESGYLQSHP CCCCCCCCCCCCCCC	34.53	23186163
231	Phosphorylation	SSDTESGYLQSHPQH CCCCCCCCCCCCCCC	15.73	23186163
234	Phosphorylation	TESGYLQSHPQHSVD CCCCCCCCCCCCCHH	34.24	23186163
239	Phosphorylation	LQSHPQHSVDRIYSA CCCCCCCCHHHHHHH	22.07	23312004
251	Phosphorylation	YSALYACSMQNGSGE HHHHHHHHCCCCCCC	18.41	28857561
268	O-linked_Glycosylation	FYSGAVVSHHETALG CCCCCEEECCHHCCC	16.72	30059200
301	Phosphorylation	RSQQMERYLSTTPET HHHHHHHHHCCCCCC	7.53	30266825
303	Phosphorylation	QQMERYLSTTPETTH HHHHHHHCCCCCCCC	22.69	30266825
304	Phosphorylation	QMERYLSTTPETTHC HHHHHHCCCCCCCCC	43.72	26657352
305	Phosphorylation	MERYLSTTPETTHCR HHHHHCCCCCCCCCC	18.76	26657352
308	Phosphorylation	YLSTTPETTHCRKQP HHCCCCCCCCCCCCC	24.04	30266825
309	Phosphorylation	LSTTPETTHCRKQPR HCCCCCCCCCCCCCC	19.81	22817900
330	Sumoylation	LVGNIHIKQEMEDDY EECCEEECCHHCCCC	26.50	25114211
330	Sumoylation	LVGNIHIKQEMEDDY EECCEEECCHHCCCC	26.50	-
353	Phosphorylation	QILERNESEECTEDT EEEECCCCCCCCCCC	42.09	28857561
357	Phosphorylation	RNESEECTEDTDQAE CCCCCCCCCCCCCCC	39.93	26657352
371	Sumoylation	EGTESEPKGESFDSG CCCCCCCCCCCCCCC	71.86	28112733
374	Phosphorylation	ESEPKGESFDSGVSS CCCCCCCCCCCCCCC	42.92	24275569
377	Phosphorylation	PKGESFDSGVSSSIG CCCCCCCCCCCCCCC	38.80	24275569
385	Phosphorylation	GVSSSIGTEPDSVEQ CCCCCCCCCCCCHHH	42.55	24275569
389	Phosphorylation	SIGTEPDSVEQQFGP CCCCCCCCHHHHCCC	37.96	24275569
402	Phosphorylation	GPGAARDSQAEPTQP CCCCCCCCCCCCCCH	26.24	22167270
407	Phosphorylation	RDSQAEPTQPEQAAE CCCCCCCCCHHHHHC	48.54	22167270
423	Phosphorylation	PAEGGPQTNQLETGA CCCCCCCCCCCCCCC	28.24	22167270
428	Phosphorylation	PQTNQLETGASSPER CCCCCCCCCCCCCCC	46.79	30266825
431	Phosphorylation	NQLETGASSPERSNE CCCCCCCCCCCCCCC	48.01	30266825
432	Phosphorylation	QLETGASSPERSNEV CCCCCCCCCCCCCCE	30.19	30266825
436	Phosphorylation	GASSPERSNEVEMDS CCCCCCCCCCEECCC	35.36	27251275
443	Phosphorylation	SNEVEMDSTVITVSN CCCEECCCEEEEEEC	24.22	27251275
444	Phosphorylation	NEVEMDSTVITVSNS CCEECCCEEEEEECC	16.21	27251275
451	Phosphorylation	TVITVSNSSDKSVLQ EEEEEECCCCCCHHC	32.19	-
461	Phosphorylation	KSVLQQPSVNTSIGQ CCHHCCCCCCCCCCC	24.54	22817900
464	O-linked_Glycosylation	LQQPSVNTSIGQPLP HCCCCCCCCCCCCCC	21.40	30059200
464	Phosphorylation	LQQPSVNTSIGQPLP HCCCCCCCCCCCCCC	21.40	22817900
465	O-linked_Glycosylation	QQPSVNTSIGQPLPS CCCCCCCCCCCCCCC	21.37	30059200
465	Phosphorylation	QQPSVNTSIGQPLPS CCCCCCCCCCCCCCC	21.37	22817900
472	Phosphorylation	SIGQPLPSTQLYLRQ CCCCCCCCCCEEEEE	36.15	22817900
480	O-linked_Glycosylation	TQLYLRQTETLTSNL CCEEEEECCCCCCCC	25.22	30059200
590	Ubiquitination	CNKTFTAKQNYVKHM CCCEEECCCCEEEEE	35.70	-
601	Phosphorylation	VKHMFVHTGEKPHQC EEEEEEECCCCCCCC	41.56	27251275
614	Phosphorylation	QCSICWRSFSLKDYL CCEEEEECCCHHHHH	8.49	24719451
616	Phosphorylation	SICWRSFSLKDYLIK EEEEECCCHHHHHHH	35.44	24719451
648	Phosphorylation	KRFTQKSSLNVHMRL CCCCCCCCCEEEEEE	30.88	24719451
685	Phosphorylation	ERHVALHSASNGTPP HHHHHHHHCCCCCCC	33.95	30266825
687	Phosphorylation	HVALHSASNGTPPAG HHHHHHCCCCCCCCC	38.51	30266825
690	Phosphorylation	LHSASNGTPPAGTPP HHHCCCCCCCCCCCC	30.28	30266825
695	Phosphorylation	NGTPPAGTPPGARAG CCCCCCCCCCCCCCC	28.54	30266825
723	Sumoylation	VCSVCPAKFDQIEQF EEEECCCCHHHHHHH	34.32	28112733

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ZBT20_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZBT20_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ZBT20_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ZBT20_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 259050: Primrose syndrome (PRIMS)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.