ZN155_HUMAN - dbPTM
ZN155_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN155_HUMAN
UniProt AC Q12901
Protein Name Zinc finger protein 155
Gene Name ZNF155
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTTFKEAVTFKDVAVVFTEEELGLLDPAQRKLYRDVMLENFRNLLSVGHQPFHQDTCHFLREEKFWMMGTATQREGNSGGKIQTELESVPEAGAHEEWSCQQIWEQIAKDLTRSQDSIINNSQFFENGDVPSQVEAGLPTIHTGQKPSQGGKCKQSISDVPIFDLPQQLYSEEKSYTCDECGKSICYISALHVHQRVHVGEKLFMCDVCGKEFSQSSHLQTHQRVHTGEKPFKCEQCGKGFSRRSALNVHRKLHTGEKPYICEACGKAFIHDSQLKEHKRIHTGEKPFKCDICGKTFYFRSRLKSHSMVHTGEKPFRCDTCDKSFHQRSALNRHCMVHTGEKPYRCEQCGKGFIGRLDFYKHQVVHTGEKPYNCKECGKSFRWSSCLLNHQRVHSGEKSFKCEECGKGFYTNSQLSSHQRSHSGEKPYKCEECGKGYVTKFNLDLHQRVHTGERPYNCKECGKNFSRASSILNHKRLHCQKKPFKCEDCGKRLVHRTYRKDQPRDYSGENPSKCEDCGRRYKRRLNLDILLSLFLNDT
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
9PhosphorylationTTFKEAVTFKDVAVV
CCHHHCEECCCEEEE
31.8326546556
18PhosphorylationKDVAVVFTEEELGLL
CCEEEEEEHHHHCCC
30.77-
31SumoylationLLDPAQRKLYRDVML
CCCHHHHHHHHHHHH
37.48-
31SumoylationLLDPAQRKLYRDVML
CCCHHHHHHHHHHHH
37.48-
227PhosphorylationQTHQRVHTGEKPFKC
CCCCCCCCCCCCCCC
44.1523898821
233SumoylationHTGEKPFKCEQCGKG
CCCCCCCCCCCCCCC
45.44-
233SumoylationHTGEKPFKCEQCGKG
CCCCCCCCCCCCCCC
45.44-
245PhosphorylationGKGFSRRSALNVHRK
CCCCCHHHHHHHHHH
35.6822817900
255PhosphorylationNVHRKLHTGEKPYIC
HHHHHCCCCCCCCEE
58.43-
258SumoylationRKLHTGEKPYICEAC
HHCCCCCCCCEECCC
44.45-
258SumoylationRKLHTGEKPYICEAC
HHCCCCCCCCEECCC
44.45-
283PhosphorylationKEHKRIHTGEKPFKC
HHCCCCCCCCCCEEC
44.6718669648
305O-linked_GlycosylationYFRSRLKSHSMVHTG
EEHHHHHHCCCEECC
25.9431492838
307O-linked_GlycosylationRSRLKSHSMVHTGEK
HHHHHHCCCEECCCC
29.5931492838
311PhosphorylationKSHSMVHTGEKPFRC
HHCCCEECCCCCCCC
35.31-
339PhosphorylationNRHCMVHTGEKPYRC
HCCCEEECCCCCCCC
35.31-
342UbiquitinationCMVHTGEKPYRCEQC
CEEECCCCCCCCCCC
49.01-
367PhosphorylationYKHQVVHTGEKPYNC
EECCEEECCCCCCCC
35.11-
429UbiquitinationHSGEKPYKCEECGKG
CCCCCCEECCCCCCE
43.63-
429SumoylationHSGEKPYKCEECGKG
CCCCCCEECCCCCCE
43.63-
429SumoylationHSGEKPYKCEECGKG
CCCCCCEECCCCCCE
43.63-
440SumoylationCGKGYVTKFNLDLHQ
CCCEEEEEEEEEHHH
23.39-
440SumoylationCGKGYVTKFNLDLHQ
CCCEEEEEEEEEHHH
23.39-
451PhosphorylationDLHQRVHTGERPYNC
EHHHHHHCCCCCCCH
37.5728555341

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 ZN155_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN155_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 ZN155_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR103_HUMANKRTAP10-3physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN155_HUMAN

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Related Literatures of Post-Translational Modification

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