ZN394_HUMAN - dbPTM
ZN394_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN394_HUMAN
UniProt AC Q53GI3
Protein Name Zinc finger protein 394
Gene Name ZNF394
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNSSLTAQRRGSDAELGPWVMAARSKDAAPSQRDGLLPVKVEEDSPGSWEPNYPAASPDPETSRLHFRQLRYQEVAGPEEALSRLRELCRRWLRPELLSKEQILELLVLEQFLTILPEELQAWVREHCPESGEEAVAVVRALQRALDGTSSQGMVTFEDTAVSLTWEEWERLDPARRDFCRESAQKDSGSTVPPSLESRVENKELIPMQQILEEAEPQGQLQEAFQGKRPLFSKCGSTHEDRVEKQSGDPLPLKLENSPEAEGLNSISDVNKNGSIEGEDSKNNELQNSARCSNLVLCQHIPKAERPTDSEEHGNKCKQSFHMVTWHVLKPHKSDSGDSFHHSSLFETQRQLHEERPYKCGNCGKSFKQRSDLFRHQRIHTGEKPYGCQECGKSFSQSAALTKHQRTHTGEKPYTCLKCGERFRQNSHLNRHQSTHSRDKHFKCEECGETCHISNLFRHQRLHKGERPYKCEECEKSFKQRSDLFKHHRIHTGEKPYGCSVCGKRFNQSATLIKHQRIHTGEKPYKCLECGERFRQSTHLIRHQRIHQNKVLSAGRGGSRL
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
3Phosphorylation-----MNSSLTAQRR
-----CCCCCCCHHC
25.9828509920
12PhosphorylationLTAQRRGSDAELGPW
CCCHHCCCCCCHHHH
31.6625159151
40SumoylationRDGLLPVKVEEDSPG
CCCCCCEEEECCCCC
41.8228112733
72PhosphorylationLHFRQLRYQEVAGPE
HHHHHHHHHHHHCHH
20.02-
83PhosphorylationAGPEEALSRLRELCR
HCHHHHHHHHHHHHH
36.00-
203SumoylationLESRVENKELIPMQQ
HHHHHCCCCCCCHHH
40.1528112733
228SumoylationLQEAFQGKRPLFSKC
HHHHHCCCCCCHHHC
39.8128112733
233PhosphorylationQGKRPLFSKCGSTHE
CCCCCCHHHCCCCHH
34.4224719451
237PhosphorylationPLFSKCGSTHEDRVE
CCHHHCCCCHHHHHH
35.7428348404
238PhosphorylationLFSKCGSTHEDRVEK
CHHHCCCCHHHHHHH
17.9928348404
247PhosphorylationEDRVEKQSGDPLPLK
HHHHHHHCCCCCCCC
57.12-
254SumoylationSGDPLPLKLENSPEA
CCCCCCCCCCCCCCC
52.3828112733
258PhosphorylationLPLKLENSPEAEGLN
CCCCCCCCCCCCCCC
18.1022199227
266PhosphorylationPEAEGLNSISDVNKN
CCCCCCCCCCCCCCC
28.6328102081
268PhosphorylationAEGLNSISDVNKNGS
CCCCCCCCCCCCCCC
35.0128102081
282SumoylationSIEGEDSKNNELQNS
CCCCCCCCCCHHCHH
75.91-
282SumoylationSIEGEDSKNNELQNS
CCCCCCCCCCHHCHH
75.9128112733
292S-nitrosylationELQNSARCSNLVLCQ
HHCHHHHHCCEEEEE
2.9424105792
298S-nitrosylationRCSNLVLCQHIPKAE
HHCCEEEEECCCCCC
1.8424105792
371PhosphorylationGKSFKQRSDLFRHQR
CCCHHHHHHHHHCCC
35.8521712546
381PhosphorylationFRHQRIHTGEKPYGC
HHCCCCCCCCCCCCC
44.6728111955
403UbiquitinationSQSAALTKHQRTHTG
CHHHHHHHHCCCCCC
38.29-
407PhosphorylationALTKHQRTHTGEKPY
HHHHHCCCCCCCCCE
19.74-
409PhosphorylationTKHQRTHTGEKPYTC
HHHCCCCCCCCCEEE
46.56-
443SumoylationHSRDKHFKCEECGET
CCCCCCCCHHHCCCC
40.2228112733
486MethylationKQRSDLFKHHRIHTG
HHHHHHHHCCCCCCC
45.88115978233
492PhosphorylationFKHHRIHTGEKPYGC
HHCCCCCCCCCCCCC
44.6728111955
520PhosphorylationIKHQRIHTGEKPYKC
EECCCCCCCCCCEEE
44.6729496963
537PhosphorylationCGERFRQSTHLIRHQ
CHHHHHHHHHHHHCH
17.34-
538PhosphorylationGERFRQSTHLIRHQR
HHHHHHHHHHHHCHH
16.62-
556MethylationNKVLSAGRGGSRL--
HCCCCCCCCCCCC--
46.12115920485

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 ZN394_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN394_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 ZN394_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBL1_HUMANCTNNBL1physical
28514442
SCND1_HUMANSCAND1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN394_HUMAN

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Related Literatures of Post-Translational Modification

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