ZN282_HUMAN - dbPTM
ZN282_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN282_HUMAN
UniProt AC Q9UDV7
Protein Name Zinc finger protein 282
Gene Name ZNF282
Organism Homo sapiens (Human).
Sequence Length 671
Subcellular Localization Nucleus .
Protein Description Binds to the U5 repressive element (U5RE) of the human T cell leukemia virus type I long terminal repeat. It recognizes the 5'-TCCACCCC-3' sequence as a core motif and exerts a strong repressive effect on HTLV-I LTR-mediated expression..
Protein Sequence MQFVSTRPQPQQLGIQGLGLDSGSWSWAQALPPEEVCHQEPALRGEMAEGMPPMQAQEWDMDARRPMPFQFPPFPDRAPVFPDRMMREPQLPTAEISLWTVVAAIQAVERKVDAQASQLLNLEGRTGTAEKKLADCEKTAVEFGNHMESKWAVLGTLLQEYGLLQRRLENLENLLRNRNFWVLRLPPGSKGEAPKVPVTFVDIAVYFSEDEWKNLDEWQKELYNNLVKENYKTLMSLDAEGSVPKPDAPVQAEPREEPCVWEQRHPEEREIPMDPEAGAEPLVPAQDASSQVKREDTLCVRGQRGLEERAIPTESITDSPISAQDLLSRIKQEEHQCVWDQQDLADRDIPTDPNSESLISAHDILSWIKQEEQPYPWGPRDSMDGELGLDSGPSDSLLMVKNPPPAPPQPQPQPQPPQPQLQSQPQPQSLPPIAVAENPGGPPSRGLLDDGFQVLPGERGSGEAPPGGDRSTGGGGGDGGGGGGGAEAGTGAGGGCGSCCPGGLRRSLLLHGARSKPYSCPECGKSFGVRKSLIIHHRSHTKERPYECAECEKSFNCHSGLIRHQMTHRGERPYKCSECEKTYSRKEHLQNHQRLHTGERPFQCALCGKSFIRKQNLLKHQRIHTGERPYTCGECGKSFRYKESLKDHLRVHSGGPGPGAPRQLPPPPERD
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
111UbiquitinationAIQAVERKVDAQASQ
HHHHHHHHHHHHHHH		30.84-
111UbiquitinationAIQAVERKVDAQASQ
HHHHHHHHHHHHHHH		30.84-
156PhosphorylationSKWAVLGTLLQEYGL
HHHHHHHHHHHHHHH		21.82-
161PhosphorylationLGTLLQEYGLLQRRL
HHHHHHHHHHHHHHH		10.5017053785
190UbiquitinationLRLPPGSKGEAPKVP
EECCCCCCCCCCCCC		67.68-
228UbiquitinationELYNNLVKENYKTLM
HHHHHHHHHHHHHHH		43.3321890473
228UbiquitinationELYNNLVKENYKTLM
HHHHHHHHHHHHHHH		43.3321890473
232UbiquitinationNLVKENYKTLMSLDA
HHHHHHHHHHHCCCC		46.9221890473
232UbiquitinationNLVKENYKTLMSLDA
HHHHHHHHHHHCCCC		46.92-
245UbiquitinationDAEGSVPKPDAPVQA
CCCCCCCCCCCCCCC		54.06-
293SumoylationQDASSQVKREDTLCV
CCCCHHCCCCCCEEE		42.29-
293UbiquitinationQDASSQVKREDTLCV
CCCCHHCCCCCCEEE		42.29-
293SumoylationQDASSQVKREDTLCV
CCCCHHCCCCCCEEE		42.2928112733
313PhosphorylationLEERAIPTESITDSP
CCCCCCCCCCCCCCC		35.9326074081
315PhosphorylationERAIPTESITDSPIS
CCCCCCCCCCCCCCC		33.0126074081
317PhosphorylationAIPTESITDSPISAQ
CCCCCCCCCCCCCHH		39.4426074081
319PhosphorylationPTESITDSPISAQDL
CCCCCCCCCCCHHHH		18.5825159151
322PhosphorylationSITDSPISAQDLLSR
CCCCCCCCHHHHHHH		24.2226074081
328PhosphorylationISAQDLLSRIKQEEH
CCHHHHHHHHHHHHH		38.9826074081
331SumoylationQDLLSRIKQEEHQCV
HHHHHHHHHHHHCCC		51.01-
331SumoylationQDLLSRIKQEEHQCV
HHHHHHHHHHHHCCC		51.01-
331UbiquitinationQDLLSRIKQEEHQCV
HHHHHHHHHHHHCCC		51.01-
369SumoylationHDILSWIKQEEQPYP
HHHHHHHHHCCCCCC		45.45-
369UbiquitinationHDILSWIKQEEQPYP
HHHHHHHHHCCCCCC		45.45-
369SumoylationHDILSWIKQEEQPYP
HHHHHHHHHCCCCCC		45.45-
382PhosphorylationYPWGPRDSMDGELGL
CCCCCCCCCCCCCCC		21.76-
391PhosphorylationDGELGLDSGPSDSLL
CCCCCCCCCCCCCEE		58.61-
394PhosphorylationLGLDSGPSDSLLMVK
CCCCCCCCCCEEEEC		43.27-
507PhosphorylationCPGGLRRSLLLHGAR
CCCHHHHHHHHCCCC		19.5527251275
515PhosphorylationLLLHGARSKPYSCPE
HHHCCCCCCCCCCCC		37.13-
516AcetylationLLHGARSKPYSCPEC
HHCCCCCCCCCCCCC		42.2826051181
518PhosphorylationHGARSKPYSCPECGK
CCCCCCCCCCCCCCC		27.0030576142
519PhosphorylationGARSKPYSCPECGKS
CCCCCCCCCCCCCCC		31.5530576142
532PhosphorylationKSFGVRKSLIIHHRS
CCCCCCCEEEEECCC		17.7827251275
597PhosphorylationQNHQRLHTGERPFQC
HHHCCCCCCCCCHHH		45.3825159151
625PhosphorylationLKHQRIHTGERPYTC
HHCCCCCCCCCCEEC		38.06-
653PhosphorylationKDHLRVHSGGPGPGA
HHHEEECCCCCCCCC		42.4625159151
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 ZN282_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN282_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 ZN282_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN282_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 ZN282_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, AND MASSSPECTROMETRY.

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