ZBT18_HUMAN - dbPTM
ZBT18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT18_HUMAN
UniProt AC Q99592
Protein Name Zinc finger and BTB domain-containing protein 18
Gene Name ZBTB18
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Nucleus. Associates with condensed chromatin.
Protein Description Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. May also play a role in the organization of chromosomes in the nucleus..
Protein Sequence MEFPDHSRHLLQCLSEQRHQGFLCDCTVLVGDAQFRAHRAVLASCSMYFHLFYKDQLDKRDIVHLNSDIVTAPAFALLLEFMYEGKLQFKDLPIEDVLAAASYLHMYDIVKVCKKKLKEKATTEADSTKKEEDASSCSDKVESLSDGSSHIAGDLPSDEDEGEDEKLNILPSKRDLAAEPGNMWMRLPSDSAGIPQAGGEAEPHATAAGKTVASPCSSTESLSQRSVTSVRDSADVDCVLDLSVKSSLSGVENLNSSYFSSQDVLRSNLVQVKVEKEASCDESDVGTNDYDMEHSTVKESVSTNNRVQYEPAHLAPLREDSVLRELDREDKASDDEMMTPESERVQVEGGMESSLLPYVSNILSPAGQIFMCPLCNKVFPSPHILQIHLSTHFREQDGIRSKPAADVNVPTCSLCGKTFSCMYTLKRHERTHSGEKPYTCTQCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCELVNSLSVKSEALSLPTVRDWTLEDSSQELWK
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
123PhosphorylationKLKEKATTEADSTKK
HHHHHCCCCCCCCCH
30576142
127PhosphorylationKATTEADSTKKEEDA
HCCCCCCCCCHHHHH
30576142
128PhosphorylationATTEADSTKKEEDAS
CCCCCCCCCHHHHHH
28258704
136PhosphorylationKKEEDASSCSDKVES
CHHHHHHHCHHHHHH
-
157PhosphorylationHIAGDLPSDEDEGED
CCCCCCCCCCCCCCH
22496350
166PhosphorylationEDEGEDEKLNILPSK
CCCCCHHHCCCCCCH
27251275
172PhosphorylationEKLNILPSKRDLAAE
HHCCCCCCHHHCCCC
24719451
189PhosphorylationNMWMRLPSDSAGIPQ
CEEEECCCCCCCCCC
29978859
191PhosphorylationWMRLPSDSAGIPQAG
EEECCCCCCCCCCCC
29978859
198PhosphorylationSAGIPQAGGEAEPHA
CCCCCCCCCCCCCCC
27251275
211PhosphorylationHATAAGKTVASPCSS
CCCCCCCEEECCCCC
27732954
214PhosphorylationAAGKTVASPCSSTES
CCCCEEECCCCCCHH
27732954
217PhosphorylationKTVASPCSSTESLSQ
CEEECCCCCCHHHHH
27732954
218PhosphorylationTVASPCSSTESLSQR
EEECCCCCCHHHHHC
27732954
219PhosphorylationVASPCSSTESLSQRS
EECCCCCCHHHHHCC
27732954
221PhosphorylationSPCSSTESLSQRSVT
CCCCCCHHHHHCCCC
27732954
223PhosphorylationCSSTESLSQRSVTSV
CCCCHHHHHCCCCCH
27732954
246PhosphorylationVLDLSVKSSLSGVEN
EEEEEECHHHCCCCC
28634120
247PhosphorylationLDLSVKSSLSGVENL
EEEEECHHHCCCCCC
28634120
249PhosphorylationLSVKSSLSGVENLNS
EEECHHHCCCCCCCC
28634120
256PhosphorylationSGVENLNSSYFSSQD
CCCCCCCCCCCCCHH
28634120
260PhosphorylationNLNSSYFSSQDVLRS
CCCCCCCCCHHHHHH
28634120
273SumoylationRSNLVQVKVEKEASC
HHCCEEEEEEECCCC
28112733
279PhosphorylationVKVEKEASCDESDVG
EEEEECCCCCHHCCC
30108239
283PhosphorylationKEASCDESDVGTNDY
ECCCCCHHCCCCCCC
30108239
287PhosphorylationCDESDVGTNDYDMEH
CCHHCCCCCCCCCCC
30108239
288PhosphorylationDESDVGTNDYDMEHS
CHHCCCCCCCCCCCC
27251275
290PhosphorylationSDVGTNDYDMEHSTV
HCCCCCCCCCCCCCC
27732954
295PhosphorylationNDYDMEHSTVKESVS
CCCCCCCCCCCCCCC
27732954
296PhosphorylationDYDMEHSTVKESVST
CCCCCCCCCCCCCCC
30177828
302PhosphorylationSTVKESVSTNNRVQY
CCCCCCCCCCCCEEE
30576142
303PhosphorylationTVKESVSTNNRVQYE
CCCCCCCCCCCEEEC
30576142
321PhosphorylationLAPLREDSVLRELDR
HHCCCCCHHHHHHCC
28348404
330PhosphorylationLRELDREDKASDDEM
HHHHCCCCCCCCCCC
27251275
333PhosphorylationLDREDKASDDEMMTP
HCCCCCCCCCCCCCC
23401153
339PhosphorylationASDDEMMTPESERVQ
CCCCCCCCCHHHCEE
27732954
342PhosphorylationDEMMTPESERVQVEG
CCCCCCHHHCEEEEC
28122231
495PhosphorylationFHCELVNSLSVKSEA
HHHHHHHHCCCCCCC
26074081
497PhosphorylationCELVNSLSVKSEALS
HHHHHHCCCCCCCCC
26074081
500PhosphorylationVNSLSVKSEALSLPT
HHHCCCCCCCCCCCC
22210691
507PhosphorylationSEALSLPTVRDWTLE
CCCCCCCCCCCCCCC
-
516PhosphorylationRDWTLEDSSQELWK-
CCCCCCCCHHHHCC-
17525332
517PhosphorylationDWTLEDSSQELWK--
CCCCCCCHHHHCC--
17525332
525PhosphorylationQELWK----------
HHHCC----------
27251275
526PhosphorylationELWK-----------
HHCC-----------
27251275

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 ZBT18_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBT18_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 ZBT18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM3A_HUMANDNMT3Aphysical
11350943
DNM3A_HUMANDNMT3Aphysical
15616584
ZBT42_HUMANZBTB42physical
28514442
ATX1L_HUMANATXN1Lphysical
28514442
CIC_HUMANCICphysical
28514442
ZN131_HUMANZNF131physical
28514442
CP4FC_HUMANCYP4F12physical
28514442
ZBTB3_HUMANZBTB3physical
28514442
RCBT2_HUMANRCBTB2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612337Mental retardation, autosomal dominant 22 (MRD22)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZBT18_HUMAN

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Related Literatures of Post-Translational Modification

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