ZN391_HUMAN - dbPTM
ZN391_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN391_HUMAN
UniProt AC Q9UJN7
Protein Name Zinc finger protein 391
Gene Name ZNF391
Organism Homo sapiens (Human).
Sequence Length 358
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MESLRGNTAQGPTNEEDYKNEGQLSRQTKCPAQKKSSFENTVVRKVSVTLKEIFTGEEGPESSEFSLSPNLDAQQKIPKGHGSPISRKNSKDNSDLIKHQRLFSQRKPCKCNECEKAFSYQSDLLVHSRIHGGEKPFECNKCGKSFSRSTHLIEHQRTHTGEKPYECNECGKAFSRSTHLSLHQRIHTGEKPYECSECGKAFSRSTNLSQHQRTHTQERPYKCNECGKAFGDRSTIIQHQRIHTGENPYECSKCGKAFSWISSLTEHQRTHTGENPYECSECGKVFSRSSSLTEHQRIHSGEKPHECRVCGKGFSRSSSLIIHQRTHTGEKPYKCNDCGKAFCQSSTLIRHQHLHTKE
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
8PhosphorylationMESLRGNTAQGPTNE
CCCCCCCCCCCCCCH		24.1524043423
13PhosphorylationGNTAQGPTNEEDYKN
CCCCCCCCCHHHHCC		63.1924043423
18PhosphorylationGPTNEEDYKNEGQLS
CCCCHHHHCCCCHHC		20.9924043423
36PhosphorylationKCPAQKKSSFENTVV
CCCCCCCCCCCCHHH		47.5022817900
41O-linked_GlycosylationKKSSFENTVVRKVSV
CCCCCCCHHHEEEEE		17.1230379171
47PhosphorylationNTVVRKVSVTLKEIF
CHHHEEEEEEEEHHH		16.6623911959
49PhosphorylationVVRKVSVTLKEIFTG
HHEEEEEEEEHHHCC		25.3029978859
83PhosphorylationKIPKGHGSPISRKNS
CCCCCCCCCCCCCCC		17.2428348404
86PhosphorylationKGHGSPISRKNSKDN
CCCCCCCCCCCCCCC		40.3517081983
147PhosphorylationNKCGKSFSRSTHLIE
CCCCCCCCCCCCHHE		32.2017081983
158PhosphorylationHLIEHQRTHTGEKPY
CHHEECCCCCCCCCE		19.7428348404
160PhosphorylationIEHQRTHTGEKPYEC
HEECCCCCCCCCEEC		46.5629496963
163UbiquitinationQRTHTGEKPYECNEC
CCCCCCCCCEECCCC		55.00-
165PhosphorylationTHTGEKPYECNECGK
CCCCCCCEECCCCCC		44.15-
188PhosphorylationSLHQRIHTGEKPYEC
CHHHHHCCCCCCEEC		44.6729496963
193PhosphorylationIHTGEKPYECSECGK
HCCCCCCEECCHHHH		40.41-
196PhosphorylationGEKPYECSECGKAFS
CCCCEECCHHHHHCC		24.7927251275
200UbiquitinationYECSECGKAFSRSTN
EECCHHHHHCCCCCC		58.90-
205PhosphorylationCGKAFSRSTNLSQHQ
HHHHCCCCCCCHHHC		22.0522468782
222SumoylationHTQERPYKCNECGKA
CCCCCCCCCCCHHHH		33.01-
222SumoylationHTQERPYKCNECGKA
CCCCCCCCCCCHHHH		33.01-
234PhosphorylationGKAFGDRSTIIQHQR
HHHHCCCCCEEECCE		28.7928555341
244PhosphorylationIQHQRIHTGENPYEC
EECCEECCCCCCCCC		43.76-
317PhosphorylationCGKGFSRSSSLIIHQ
CCCCCCCCCEEEEEE		24.0723186163
318PhosphorylationGKGFSRSSSLIIHQR
CCCCCCCCEEEEEEC		28.2223186163
319PhosphorylationKGFSRSSSLIIHQRT
CCCCCCCEEEEEECC		25.4925106551
326PhosphorylationSLIIHQRTHTGEKPY
EEEEEECCCCCCCCE		19.7428348404
328PhosphorylationIIHQRTHTGEKPYKC
EEEECCCCCCCCEEC		46.5624719451
331UbiquitinationQRTHTGEKPYKCNDC
ECCCCCCCCEECCCH		55.80-
331AcetylationQRTHTGEKPYKCNDC
ECCCCCCCCEECCCH		55.807428917
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 ZN391_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN391_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 ZN391_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN391_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 ZN391_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-49, AND MASSSPECTROMETRY.

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