ZBT34_HUMAN - dbPTM
ZBT34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT34_HUMAN
UniProt AC Q8NCN2
Protein Name Zinc finger and BTB domain-containing protein 34
Gene Name ZBTB34
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Nucleus .
Protein Description May be a transcriptional repressor..
Protein Sequence MDSSSFIQFDVPEYSSTVLSQLNELRLQGKLCDIIVHIQGQPFRAHKAVLAASSPYFRDHSALSTMSGLSISVIKNPNVFEQLLSFCYTGRMSLQLKDVVSFLTAASFLQMQCVIDKCTQILESIHSKISVGDVDSVTVGAEENPESRNGVKDSSFFANPVEISPPYCSQGRQPTASSDLRMETTPSKALRSRLQEEGHSDRGSSGSVSEYEIQIEGDHEQGDLLVRESQITEVKVKMEKSDRPSCSDSSSLGDDGYHTEMVDGEQVVAVNVGSYGSVLQHAYSYSQAASQPTNVSEAFGSLSNSSPSRSMLSCFRGGRARQKRALSVHLHSDLQGLVQGSDSEAMMNNPGYESSPRERSARGHWYPYNERLICIYCGKSFNQKGSLDRHMRLHMGITPFVCKFCGKKYTRKDQLEYHIRGHTDDKPFRCEICGKCFPFQGTLNQHLRKNHPGVAEVRSRIESPERTDVYVEQKLENDASASEMGLDSRMEIHTVSDAPD
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
30UbiquitinationNELRLQGKLCDIIVH
HHHHHCCCCCCEEEE
32.74-
119PhosphorylationQCVIDKCTQILESIH
HHHHHHHHHHHHHHH
25.1225690035
124PhosphorylationKCTQILESIHSKISV
HHHHHHHHHHCCCCC
23.3525690035
152UbiquitinationPESRNGVKDSSFFAN
CCCCCCCCCCCCCCC
53.98-
154PhosphorylationSRNGVKDSSFFANPV
CCCCCCCCCCCCCCC
24.2726074081
155PhosphorylationRNGVKDSSFFANPVE
CCCCCCCCCCCCCCE
34.2226074081
164PhosphorylationFANPVEISPPYCSQG
CCCCCEECCCCCCCC
13.3023401153
167PhosphorylationPVEISPPYCSQGRQP
CCEECCCCCCCCCCC
14.2326074081
169PhosphorylationEISPPYCSQGRQPTA
EECCCCCCCCCCCCC
29.8126074081
185PhosphorylationSDLRMETTPSKALRS
CCCCCCCCCCHHHHH
16.5625627689
188UbiquitinationRMETTPSKALRSRLQ
CCCCCCCHHHHHHHH
53.28-
188AcetylationRMETTPSKALRSRLQ
CCCCCCCHHHHHHHH
53.2825953088
207PhosphorylationSDRGSSGSVSEYEIQ
CCCCCCCCEEEEEEE
25.1524247654
235SumoylationESQITEVKVKMEKSD
HHHCEEEEEEECCCC
29.8828112733
237SumoylationQITEVKVKMEKSDRP
HCEEEEEEECCCCCC
35.3128112733
332PhosphorylationALSVHLHSDLQGLVQ
EEEEEECHHHHHHHC
46.5024247654
362MethylationSPRERSARGHWYPYN
CCCHHCCCCCCCCCC
38.46115920313
380PhosphorylationICIYCGKSFNQKGSL
EEEECCCCCCCCCCH
18.0823401153
384UbiquitinationCGKSFNQKGSLDRHM
CCCCCCCCCCHHHHH
52.12-
386PhosphorylationKSFNQKGSLDRHMRL
CCCCCCCCHHHHHHH
33.8524719451
412UbiquitinationCGKKYTRKDQLEYHI
CCCCCCCHHHHHHEE
41.86-
423PhosphorylationEYHIRGHTDDKPFRC
HHEECCCCCCCCEEE
49.0328674419
426SumoylationIRGHTDDKPFRCEIC
ECCCCCCCCEEEEEC
49.1928112733
459PhosphorylationPGVAEVRSRIESPER
CCHHHHHHHCCCCCC
42.6723403867
463PhosphorylationEVRSRIESPERTDVY
HHHHHCCCCCCCCEE
29.6823401153
467PhosphorylationRIESPERTDVYVEQK
HCCCCCCCCEEEEHH
28.3123403867
470PhosphorylationSPERTDVYVEQKLEN
CCCCCCEEEEHHHHC
10.9023403867
474SumoylationTDVYVEQKLENDASA
CCEEEEHHHHCCCCH
44.2428112733
494PhosphorylationDSRMEIHTVSDAPD-
CCCEEEEECCCCCC-
27.6328450419
496PhosphorylationRMEIHTVSDAPD---
CEEEEECCCCCC---
29.2528450419

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 ZBT34_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBT34_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 ZBT34_HUMAN !!

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

Oops, there are no PPI records of ZBT34_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZBT34_HUMAN

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Related Literatures of Post-Translational Modification

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