OZF_HUMAN - dbPTM
OZF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OZF_HUMAN
UniProt AC Q15072
Protein Name Zinc finger protein OZF
Gene Name ZNF146
Organism Homo sapiens (Human).
Sequence Length 292
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MSHLSQQRIYSGENPFACKVCGKVFSHKSNLTEHEHFHTREKPFECNECGKAFSQKQYVIKHQNTHTGEKLFECNECGKSFSQKENLLTHQKIHTGEKPFECKDCGKAFIQKSNLIRHQRTHTGEKPFVCKECGKTFSGKSNLTEHEKIHIGEKPFKCSECGTAFGQKKYLIKHQNIHTGEKPYECNECGKAFSQRTSLIVHVRIHSGDKPYECNVCGKAFSQSSSLTVHVRSHTGEKPYGCNECGKAFSQFSTLALHLRIHTGKKPYQCSECGKAFSQKSHHIRHQKIHTH
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
11PhosphorylationLSQQRIYSGENPFAC
CCCCCHHCCCCCHHH
36.9425159151
19UbiquitinationGENPFACKVCGKVFS
CCCCHHHHHCCEEEC
36.8132015554
23UbiquitinationFACKVCGKVFSHKSN
HHHHHCCEEECCCCC
34.6729967540
28SumoylationCGKVFSHKSNLTEHE
CCEEECCCCCCCCCC
39.58-
28UbiquitinationCGKVFSHKSNLTEHE
CCEEECCCCCCCCCC
39.5829967540
28SumoylationCGKVFSHKSNLTEHE
CCEEECCCCCCCCCC
39.5828112733
42UbiquitinationEHFHTREKPFECNEC
CCCCCCCCCCCCCCC
52.28-
51SumoylationFECNECGKAFSQKQY
CCCCCCCCCHHHCEE
58.90-
51SumoylationFECNECGKAFSQKQY
CCCCCCCCCHHHCEE
58.9028112733
56SumoylationCGKAFSQKQYVIKHQ
CCCCHHHCEEEEEEC
42.26-
56UbiquitinationCGKAFSQKQYVIKHQ
CCCCHHHCEEEEEEC
42.2633845483
56SumoylationCGKAFSQKQYVIKHQ
CCCCHHHCEEEEEEC
42.2628112733
61SumoylationSQKQYVIKHQNTHTG
HHCEEEEEECCCCCC
29.15-
61SumoylationSQKQYVIKHQNTHTG
HHCEEEEEECCCCCC
29.15-
70UbiquitinationQNTHTGEKLFECNEC
CCCCCCCEEEEECCC
60.8832015554
79UbiquitinationFECNECGKSFSQKEN
EEECCCCCCCCHHHC
61.05-
84SumoylationCGKSFSQKENLLTHQ
CCCCCCHHHCCCCCC
47.58-
84UbiquitinationCGKSFSQKENLLTHQ
CCCCCCHHHCCCCCC
47.5832015554
84SumoylationCGKSFSQKENLLTHQ
CCCCCCHHHCCCCCC
47.58-
92UbiquitinationENLLTHQKIHTGEKP
HCCCCCCCCCCCCCC
28.9329967540
95PhosphorylationLTHQKIHTGEKPFEC
CCCCCCCCCCCCCCC
50.9724719451
103UbiquitinationGEKPFECKDCGKAFI
CCCCCCCCCHHHHHH
49.18-
107UbiquitinationFECKDCGKAFIQKSN
CCCCCHHHHHHHHHC
46.5923000965
112SumoylationCGKAFIQKSNLIRHQ
HHHHHHHHHCCCEEC
36.17-
112SumoylationCGKAFIQKSNLIRHQ
HHHHHHHHHCCCEEC
36.17-
112UbiquitinationCGKAFIQKSNLIRHQ
HHHHHHHHHCCCEEC
36.1723000965
121PhosphorylationNLIRHQRTHTGEKPF
CCCEECCCCCCCCCE
19.7422210691
123PhosphorylationIRHQRTHTGEKPFVC
CEECCCCCCCCCEEE
46.5629214152
126SumoylationQRTHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.13-
126SumoylationQRTHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.13-
126UbiquitinationQRTHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.1329967540
126AcetylationQRTHTGEKPFVCKEC
CCCCCCCCCEEECCC
45.1326822725
131UbiquitinationGEKPFVCKECGKTFS
CCCCEEECCCCCCCC
51.2233845483
135AcetylationFVCKECGKTFSGKSN
EEECCCCCCCCCCCC
59.0461273
140AcetylationCGKTFSGKSNLTEHE
CCCCCCCCCCCCCCC
34.6770891
140SumoylationCGKTFSGKSNLTEHE
CCCCCCCCCCCCCCC
34.67-
140UbiquitinationCGKTFSGKSNLTEHE
CCCCCCCCCCCCCCC
34.6732015554
140SumoylationCGKTFSGKSNLTEHE
CCCCCCCCCCCCCCC
34.67-
148UbiquitinationSNLTEHEKIHIGEKP
CCCCCCCEEECCCCC
41.3029967540
157SumoylationHIGEKPFKCSECGTA
ECCCCCEECCCCCCC
45.43-
157SumoylationHIGEKPFKCSECGTA
ECCCCCEECCCCCCC
45.43-
157UbiquitinationHIGEKPFKCSECGTA
ECCCCCEECCCCCCC
45.4329967540
169SumoylationGTAFGQKKYLIKHQN
CCCCCCEEEEEECCC
37.08-
169UbiquitinationGTAFGQKKYLIKHQN
CCCCCCEEEEEECCC
37.08-
169SumoylationGTAFGQKKYLIKHQN
CCCCCCEEEEEECCC
37.08-
173SumoylationGQKKYLIKHQNIHTG
CCEEEEEECCCCCCC
36.22-
173SumoylationGQKKYLIKHQNIHTG
CCEEEEEECCCCCCC
36.2228112733
173UbiquitinationGQKKYLIKHQNIHTG
CCEEEEEECCCCCCC
36.2229967540
179PhosphorylationIKHQNIHTGEKPYEC
EECCCCCCCCCCCCC
43.1528152594
182UbiquitinationQNIHTGEKPYECNEC
CCCCCCCCCCCCCCC
55.0029967540
184PhosphorylationIHTGEKPYECNECGK
CCCCCCCCCCCCCCC
44.1528152594
191UbiquitinationYECNECGKAFSQRTS
CCCCCCCCHHHCCCE
58.90-
197PhosphorylationGKAFSQRTSLIVHVR
CCHHHCCCEEEEEEE
21.9029214152
198PhosphorylationKAFSQRTSLIVHVRI
CHHHCCCEEEEEEEE
20.4929214152
204MethylationTSLIVHVRIHSGDKP
CEEEEEEEEECCCCC
13.16-
207PhosphorylationIVHVRIHSGDKPYEC
EEEEEEECCCCCEEE
46.4425159151
210UbiquitinationVRIHSGDKPYECNVC
EEEECCCCCEEECCC
53.69-
235PhosphorylationTVHVRSHTGEKPYGC
EEEEEECCCCCCCCC
48.5629496963
238UbiquitinationVRSHTGEKPYGCNEC
EEECCCCCCCCCCCC
44.90-
263PhosphorylationALHLRIHTGKKPYQC
HHHHHHHCCCCCEEC
48.61-
265UbiquitinationHLRIHTGKKPYQCSE
HHHHHCCCCCEECCH
52.29-
265AcetylationHLRIHTGKKPYQCSE
HHHHHCCCCCEECCH
52.2925953088
266UbiquitinationLRIHTGKKPYQCSEC
HHHHCCCCCEECCHH
50.75-
266SumoylationLRIHTGKKPYQCSEC
HHHHCCCCCEECCHH
50.75-
266SumoylationLRIHTGKKPYQCSEC
HHHHCCCCCEECCHH
50.75-
275UbiquitinationYQCSECGKAFSQKSH
EECCHHHHHHHCCCH
58.9029967540
275AcetylationYQCSECGKAFSQKSH
EECCHHHHHHHCCCH
58.9012432485
280SumoylationCGKAFSQKSHHIRHQ
HHHHHHCCCHHHHCC
51.03-
280UbiquitinationCGKAFSQKSHHIRHQ
HHHHHHCCCHHHHCC
51.0329967540
280SumoylationCGKAFSQKSHHIRHQ
HHHHHHCCCHHHHCC
51.03-
280AcetylationCGKAFSQKSHHIRHQ
HHHHHHCCCHHHHCC
51.0312432495

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 OZF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OZF_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 OZF_HUMAN !!

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

Oops, there are no PPI records of OZF_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 OZF_HUMAN

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Related Literatures of Post-Translational Modification

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