ZN121_HUMAN - dbPTM
ZN121_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN121_HUMAN
UniProt AC P58317
Protein Name Zinc finger protein 121
Gene Name ZNF121
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAEIHNGGELCDFMENGEIFSEHSCLNAHMGTENTGDTYDCDEYGENFPMLHNSAPAGETLSVLNQCRKAFSLPPNVHQRTWIGDKSFEYSDCEEAFVDQSHLQANRITHNGETLYEQKQCGRAFTYSTSHAVSVKMHTVEKPYECKECGKFFRYSSYLNSHMRTHTGEKPYECKECGKCFTVSSHLVEHVRIHTGEKPYQCKECGRAFAGRSGLTKHVRIHTGEKPYECNECGKAYNRFYLLTEHFKTHTEEKPFECKVCGKSFRSSSCLKNHFRIHTGIKPYKCKECGKAFTVSSSLHNHVKIHTGEKPYECKDCGKAFATSSQLIEHIRTHTGEKPYICKECGKTFRASSHLQKHVRIHTGEKPYICNECGKAYNRFYLLTKHLKTH
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
69MethylationSVLNQCRKAFSLPPN
HHHHHHHHHHCCCCC		62.50115978305
69UbiquitinationSVLNQCRKAFSLPPN
HHHHHHHHHHCCCCC		62.5029967540
81PhosphorylationPPNVHQRTWIGDKSF
CCCCCCCCEECCCCC		18.1825841592
86UbiquitinationQRTWIGDKSFEYSDC
CCCEECCCCCCCCCH		52.4029967540
87PhosphorylationRTWIGDKSFEYSDCE
CCEECCCCCCCCCHH		28.2228450419
90PhosphorylationIGDKSFEYSDCEEAF
ECCCCCCCCCHHHHC		14.0628450419
91PhosphorylationGDKSFEYSDCEEAFV
CCCCCCCCCHHHHCC		28.6925159151
101PhosphorylationEEAFVDQSHLQANRI
HHHCCCHHHHHHCEE		23.0027732954
114PhosphorylationRITHNGETLYEQKQC
EECCCCCEEEEECCC		35.72-
116PhosphorylationTHNGETLYEQKQCGR
CCCCCEEEEECCCCC		24.59-
119UbiquitinationGETLYEQKQCGRAFT
CCEEEEECCCCCCEE		35.3029967540
127PhosphorylationQCGRAFTYSTSHAVS
CCCCCEEEECCCEEE		11.9627642862
128PhosphorylationCGRAFTYSTSHAVSV
CCCCEEEECCCEEEE		22.0028555341
130PhosphorylationRAFTYSTSHAVSVKM
CCEEEECCCEEEEEE		11.9630576142
134PhosphorylationYSTSHAVSVKMHTVE
EECCCEEEEEEEECC		19.4623186163
147UbiquitinationVEKPYECKECGKFFR
CCCCEECCCCCCCEE		44.06-
147SumoylationVEKPYECKECGKFFR
CCCCEECCCCCCCEE		44.06-
147SumoylationVEKPYECKECGKFFR
CCCCEECCCCCCCEE		44.06-
151UbiquitinationYECKECGKFFRYSSY
EECCCCCCCEEHHHH		53.65-
155PhosphorylationECGKFFRYSSYLNSH
CCCCCEEHHHHHHHH		9.2328152594
156PhosphorylationCGKFFRYSSYLNSHM
CCCCEEHHHHHHHHH		14.3028152594
165PhosphorylationYLNSHMRTHTGEKPY
HHHHHHCCCCCCCCC		19.0629396449
167PhosphorylationNSHMRTHTGEKPYEC
HHHHCCCCCCCCCCC		46.5629496963
170UbiquitinationMRTHTGEKPYECKEC
HCCCCCCCCCCCCCC		55.0022505724
175SumoylationGEKPYECKECGKCFT
CCCCCCCCCCCCEEE		44.06-
175UbiquitinationGEKPYECKECGKCFT
CCCCCCCCCCCCEEE		44.06-
175SumoylationGEKPYECKECGKCFT
CCCCCCCCCCCCEEE		44.06-
179UbiquitinationYECKECGKCFTVSSH
CCCCCCCCEEEEEHH		37.52-
195PhosphorylationVEHVRIHTGEKPYQC
EEEEEECCCCCCEEC		44.6728111955
203UbiquitinationGEKPYQCKECGRAFA
CCCCEECCCCCCEEC		40.28-
223PhosphorylationTKHVRIHTGEKPYEC
CCEEEEECCCCCEEE		44.6728152594
226UbiquitinationVRIHTGEKPYECNEC
EEEECCCCCEEECCC		55.00-
228PhosphorylationIHTGEKPYECNECGK
EECCCCCEEECCCHH		44.1528152594
235UbiquitinationYECNECGKAYNRFYL
EEECCCHHHHHHHHH		60.4022505724
235SumoylationYECNECGKAYNRFYL
EEECCCHHHHHHHHH		60.40-
235SumoylationYECNECGKAYNRFYL
EEECCCHHHHHHHHH		60.40-
254SumoylationFKTHTEEKPFECKVC
HHCCCCCCCCEEEEC		49.10-
254SumoylationFKTHTEEKPFECKVC
HHCCCCCCCCEEEEC		49.10-
259UbiquitinationEEKPFECKVCGKSFR
CCCCCEEEECCCCCC		33.10-
263UbiquitinationFECKVCGKSFRSSSC
CEEEECCCCCCCCHH		41.09-
272UbiquitinationFRSSSCLKNHFRIHT
CCCCHHHHHCEEEEC		53.3429967540
279PhosphorylationKNHFRIHTGIKPYKC
HHCEEEECCCCCEEC		37.9320058876
291SumoylationYKCKECGKAFTVSSS
EECCCCCCEEEEEHH		52.57-
291SumoylationYKCKECGKAFTVSSS
EECCCCCCEEEEEHH		52.57-
297PhosphorylationGKAFTVSSSLHNHVK
CCEEEEEHHHCCCCE		32.3628555341
298PhosphorylationKAFTVSSSLHNHVKI
CEEEEEHHHCCCCEE		26.5828555341
307PhosphorylationHNHVKIHTGEKPYEC
CCCCEEECCCCCEEC		50.9729496963
315UbiquitinationGEKPYECKDCGKAFA
CCCCEECCCCHHEEE		44.08-
315SumoylationGEKPYECKDCGKAFA
CCCCEECCCCHHEEE		44.08-
315SumoylationGEKPYECKDCGKAFA
CCCCEECCCCHHEEE		44.08-
333PhosphorylationQLIEHIRTHTGEKPY
HHHHHHHHHCCCCCE		24.16-
335PhosphorylationIEHIRTHTGEKPYIC
HHHHHHHCCCCCEEE		46.5628674419
338SumoylationIRTHTGEKPYICKEC
HHHHCCCCCEEECHH		44.45-
338SumoylationIRTHTGEKPYICKEC
HHHHCCCCCEEECHH		44.45-
338UbiquitinationIRTHTGEKPYICKEC
HHHHCCCCCEEECHH		44.45-
343UbiquitinationGEKPYICKECGKTFR
CCCCEEECHHCCEEE		46.62-
363PhosphorylationQKHVRIHTGEKPYIC
HHCEEEECCCCCEEE		44.6721712546
368PhosphorylationIHTGEKPYICNECGK
EECCCCCEEECCCHH		29.22-
375UbiquitinationYICNECGKAYNRFYL
EEECCCHHHHHHHHH		60.40-
385UbiquitinationNRFYLLTKHLKTH--
HHHHHHHHHHCCC--		47.0821890473
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 ZN121_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN121_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 ZN121_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN121_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 ZN121_HUMAN

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Related Literatures of Post-Translational Modification

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