ZNF28_HUMAN - dbPTM
ZNF28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF28_HUMAN
UniProt AC P17035
Protein Name Zinc finger protein 28
Gene Name ZNF28
Organism Homo sapiens (Human).
Sequence Length 718
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMMKTFFSTGQGNTEAFHTGTLQRQASHHIGDFCFQKIEKDIHGFQFQWKEDETNDHAAPMTEIKELTGSTGQHDQRHAGNKHIKDQLGLSFHSHLPELHIFQPEGKIGNQVEKSINNASSVSTSQRICCRPKTHISNKYGNNSLHSSLLTQKRNVHMREKSFQCIESGKSFNCSSLLKKHQITHLEEKQCKCDVYGKVFNQKRYLACHRRSHIDEKPYKCNECGKIFGHNTSLFLHKALHTADKPYECEECDKVFSRKSHLETHKIIYTGGKPYKCKVCDKAFTCNSYLAKHTIIHTGEKPYKCNECGKVFNRLSTLARHRRLHTGEKPYECEECEKVFSRKSHLERHKRIHTGEKPYKCKVCDKAFAYNSYLAKHSIIHTGEKPYKCNECGKVFNQQSTLARHHRLHTAEKPYKCEECDKVFRCKSHLERHRRIHTGEKPYKCKVCDKAFRSDSCLTEHQRVHTGEKPYMCNECGKVFSTKANLACHHKLHTAEKPYKCEECEKVFSRKSHMERHRRIHTGEKPYKCKVCDKAFRRDSHLAQHQRVHTGEKPYKCNECGKTFRQTSSLIIHRRLHTGEKPYKCNECGKTFSQMSSLVYHHRLHSGEKPYKCNECGKVFNQQAHLAQHQRVHTGEKPYKCNECGKTFSQMSNLVYHHRLHSGEKP
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
18PhosphorylationRDVAIEFSQEEWKCL
HHHHHCCCHHHHHHC
24.7227251275
23UbiquitinationEFSQEEWKCLDPAQR
CCCHHHHHHCCHHHH
28.35-
41PhosphorylationRDVMLENYRNLVSLD
HHHHHHHHHHHEECC
7.4822210691
46PhosphorylationENYRNLVSLDISSKC
HHHHHHEECCCCCCH
24.4022210691
79PhosphorylationGTLQRQASHHIGDFC
HHHHHHHHHHHCHHH
13.7828555341
89SumoylationIGDFCFQKIEKDIHG
HCHHHHHHHHCCCCC
32.3628112733
113 (in isoform 2)Ubiquitination-4.5021906983
166UbiquitinationKIGNQVEKSINNASS
CHHHHHHHHHHCCCC
58.7529967540
167PhosphorylationIGNQVEKSINNASSV
HHHHHHHHHHCCCCC
19.6228555341
187 (in isoform 1)Ubiquitination-27.8321906983
191UbiquitinationPKTHISNKYGNNSLH
CCCCCCCCCCCCCHH
47.9829967540
203PhosphorylationSLHSSLLTQKRNVHM
CHHHHHHHHCCCCCC
37.02-
213UbiquitinationRNVHMREKSFQCIES
CCCCCCHHHHHHHHC
46.3229967540
222UbiquitinationFQCIESGKSFNCSSL
HHHHHCCCCCCHHHH
62.2429967540
223PhosphorylationQCIESGKSFNCSSLL
HHHHCCCCCCHHHHH
25.8029970186
228PhosphorylationGKSFNCSSLLKKHQI
CCCCCHHHHHHHHCC
39.6624719451
269SumoylationRRSHIDEKPYKCNEC
CCCCCCCCCEECCCC
50.31-
269SumoylationRRSHIDEKPYKCNEC
CCCCCCCCCEECCCC
50.31-
272SumoylationHIDEKPYKCNECGKI
CCCCCCEECCCCCCC
38.83-
272SumoylationHIDEKPYKCNECGKI
CCCCCCEECCCCCCC
38.83-
321PhosphorylationLETHKIIYTGGKPYK
HCCCEEEEECCCCCC
11.6429496907
327PhosphorylationIYTGGKPYKCKVCDK
EEECCCCCCCEECCC
32.29-
340PhosphorylationDKAFTCNSYLAKHTI
CCCEECCHHHHHCCE
24.5430631047
350PhosphorylationAKHTIIHTGEKPYKC
HHCCEEECCCCCEEC
36.3129496963
353UbiquitinationTIIHTGEKPYKCNEC
CEEECCCCCEECCCH
55.80-
355PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCHHH
38.9618767875
356SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCHHHH
38.83-
356SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCHHHH
38.83-
368PhosphorylationGKVFNRLSTLARHRR
HHHHHHHHHHHHHCC
20.3824945436
378PhosphorylationARHRRLHTGEKPYEC
HHHCCCCCCCCCCCC
52.1821857030
406PhosphorylationERHKRIHTGEKPYKC
HHHCCCCCCCCCCCC
44.6729496963
411PhosphorylationIHTGEKPYKCKVCDK
CCCCCCCCCCCCCCC
39.83-
428SumoylationAYNSYLAKHSIIHTG
HCCHHHHHCCCEECC
34.9828112733
434PhosphorylationAKHSIIHTGEKPYKC
HHCCCEECCCCCEEC
36.3129496963
437SumoylationSIIHTGEKPYKCNEC
CCEECCCCCEECCCC
55.80-
437SumoylationSIIHTGEKPYKCNEC
CCEECCCCCEECCCC
55.80-
437UbiquitinationSIIHTGEKPYKCNEC
CCEECCCCCEECCCC
55.80-
439PhosphorylationIHTGEKPYKCNECGK
EECCCCCEECCCCCC
38.9618767875
440SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCCCCC
38.83-
440SumoylationHTGEKPYKCNECGKV
ECCCCCEECCCCCCC
38.83-
468SumoylationHTAEKPYKCEECDKV
CCCCCCCCHHHCCCE
43.63-
468SumoylationHTAEKPYKCEECDKV
CCCCCCCCHHHCCCE
43.63-
480PhosphorylationDKVFRCKSHLERHRR
CCEEECHHHHHHHCC
36.6127282143
490PhosphorylationERHRRIHTGEKPYKC
HHHCCCCCCCCCCCC
44.6729496963
495PhosphorylationIHTGEKPYKCKVCDK
CCCCCCCCCCCCCCH
39.83-
502UbiquitinationYKCKVCDKAFRSDSC
CCCCCCCHHHCCCCC
44.27-
518PhosphorylationTEHQRVHTGEKPYMC
CCCCCHHCCCCCEEE
44.15-
534PhosphorylationECGKVFSTKANLACH
CCCCEEEHHHHHHHC
23.78-
574PhosphorylationERHRRIHTGEKPYKC
HHHHCCCCCCCCCCC
44.6729496963
579PhosphorylationIHTGEKPYKCKVCDK
CCCCCCCCCCCCCCH
39.83-
586UbiquitinationYKCKVCDKAFRRDSH
CCCCCCCHHHHCCHH
44.27-
602PhosphorylationAQHQRVHTGEKPYKC
HHHCCCCCCCCCEEC
44.1529496963
605SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
605SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
605UbiquitinationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
608SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
608UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
608SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
619UbiquitinationCGKTFRQTSSLIIHR
CCCCHHHCCEEEEEE
18.9421890473
630PhosphorylationIIHRRLHTGEKPYKC
EEEEECCCCCCCEEC
52.1827422710
633SumoylationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.80-
633UbiquitinationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.8021890473
633SumoylationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.80-
635PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC
38.96-
636SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
636UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
636SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
658PhosphorylationVYHHRLHSGEKPYKC
HHHHCCCCCCCCEEC
53.9227794612
664SumoylationHSGEKPYKCNECGKV
CCCCCCEECCCHHHH
38.83-
664SumoylationHSGEKPYKCNECGKV
CCCCCCEECCCHHHH
38.83-
686PhosphorylationAQHQRVHTGEKPYKC
HHHCCCCCCCCCEEC
44.1529496963
689SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
689SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
689UbiquitinationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
692UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
692SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
692SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
699PhosphorylationKCNECGKTFSQMSNL
ECCCCCCCHHHHHHH
17.5025404012
701PhosphorylationNECGKTFSQMSNLVY
CCCCCCHHHHHHHHH
30.1525404012
704PhosphorylationGKTFSQMSNLVYHHR
CCCHHHHHHHHHHHC
21.2625404012
708PhosphorylationSQMSNLVYHHRLHSG
HHHHHHHHHHCCCCC
8.6225404012
714PhosphorylationVYHHRLHSGEKP---
HHHHCCCCCCCC---
53.9225404012

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 ZNF28_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF28_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 ZNF28_HUMAN !!

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

Oops, there are no PPI records of ZNF28_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZNF28_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP