ZN138_HUMAN - dbPTM
ZN138_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN138_HUMAN
UniProt AC P52744
Protein Name Zinc finger protein 138
Gene Name ZNF138
Organism Homo sapiens (Human).
Sequence Length 262
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation as a repressor..
Protein Sequence MKRHEMVVAKHSALCSRFAQDLWLEQNIKDSFQKVTLSRYGKYGHKNLQLRKGCKSVDECKGHQGGFNGLNQCLKITTSKIFQCNKYVKVMHKFSNSNRHKIRHTENKHFRCKECDKSLCMLSRLTQHKKIHTRENFYKCEECGKTFNWSTNLSKPKKIHTGEKPYKCEVCGKAFHQSSILTKHKIIRTGEKPYKCAHCGKAFKQSSHLTRHKIIHTEEKPYKCEQCGKVFKQSPTLTKHQIIYTGEEPYKCEECGKAFNLS
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
117UbiquitinationFRCKECDKSLCMLSR
CCCCCCCHHHHHHHH
57.92-
118PhosphorylationRCKECDKSLCMLSRL
CCCCCCHHHHHHHHH
17.3522210691
139UbiquitinationHTRENFYKCEECGKT
CCCCCEEECHHHCCE
30.91-
139SumoylationHTRENFYKCEECGKT
CCCCCEEECHHHCCE
30.91-
154PhosphorylationFNWSTNLSKPKKIHT
EECCCCCCCCCCCCC
49.3224719451
161PhosphorylationSKPKKIHTGEKPYKC
CCCCCCCCCCCCEEE
50.9729496963
167SumoylationHTGEKPYKCEVCGKA
CCCCCCEEEEECCCC
32.23-
170UbiquitinationEKPYKCEVCGKAFHQ
CCCEEEEECCCCHHC
7.95-
170SumoylationEKPYKCEVCGKAFHQ
CCCEEEEECCCCHHC
7.95-
179PhosphorylationGKAFHQSSILTKHKI
CCCHHCCCCHHHCCE
18.3024719451
183AcetylationHQSSILTKHKIIRTG
HCCCCHHHCCEEECC
39.1819818627
185AcetylationSSILTKHKIIRTGEK
CCCHHHCCEEECCCC
41.1919818633
189UbiquitinationTKHKIIRTGEKPYKC
HHCCEEECCCCCCCC
39.01-
192PhosphorylationKIIRTGEKPYKCAHC
CEEECCCCCCCCCCC
55.80-
198SumoylationEKPYKCAHCGKAFKQ
CCCCCCCCCCCHHHC
30.27-
198UbiquitinationEKPYKCAHCGKAFKQ
CCCCCCCCCCCHHHC
30.27-
220SumoylationKIIHTEEKPYKCEQC
CEEECCCCCCCCHHC
47.63-
223SumoylationHTEEKPYKCEQCGKV
ECCCCCCCCHHCCCE
39.56-
234PhosphorylationCGKVFKQSPTLTKHQ
CCCEECCCCCCCCCE
22.05-
238PhosphorylationFKQSPTLTKHQIIYT
ECCCCCCCCCEEEEC
29.03-
244PhosphorylationLTKHQIIYTGEEPYK
CCCCEEEECCCCCEE
15.43-
251SumoylationYTGEEPYKCEECGKA
ECCCCCEECCCCCCC
45.98-
251SumoylationYTGEEPYKCEECGKA
ECCCCCEECCCCCCC
45.98-
254SumoylationEEPYKCEECGKAFNL
CCCEECCCCCCCCCC
59.02-
275Phosphorylation--------------------
--------------------
-
282Sumoylation---------------------------
---------------------------
-
282Ubiquitination---------------------------
---------------------------
-

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 ZN138_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN138_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 ZN138_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI41_HUMANTRIM41physical
25416956
K1C40_HUMANKRT40physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN138_HUMAN

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Related Literatures of Post-Translational Modification

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