ZNF45_HUMAN - dbPTM
ZNF45_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF45_HUMAN
UniProt AC Q02386
Protein Name Zinc finger protein 45
Gene Name ZNF45
Organism Homo sapiens (Human).
Sequence Length 682
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTKSKEAVTFKDVAVVFSEEELQLLDLAQRKLYRDVMLENFRNVVSVGHQSTPDGLPQLEREEKLWMMKMATQRDNSSGAKNLKEMETLQEVGLRYLPHEELFCSQIWQQITRELIKYQDSVVNIQRTGCQLEKRDDLHYKDEGFSNQSSHLQVHRVHTGEKPYKGEHCVKSFSWSSHLQINQRAHAGEKPYKCEKCDNAFRRFSSLQAHQRVHSRAKSYTNDASYRSFSQRSHLPHHQRVPTGENPYKYEECGRNVGKSSHCQAPLIVHTGEKPYKCEECGVGFSQRSYLQVHLKVHTGKKPYKCEECGKSFSWRSRLQAHERIHTGEKPYKCNACGKSFSYSSHLNIHCRIHTGEKPYKCEECGKGFSVGSHLQAHQISHTGEKPYKCEECGKGFCRASNLLDHQRGHTGEKPYQCDACGKGFSRSSDFNIHFRVHTGEKPYKCEECGKGFSQASNLLAHQRGHTGEKPYKCGTCGKGFSRSSDLNVHCRIHTGEKPYKCERCGKAFSQFSSLQVHQRVHTGEKPYQCAECGKGFSVGSQLQAHQRCHTGEKPYQCEECGKGFCRASNFLAHRGVHTGEKPYRCDVCGKRFRQRSYLQAHQRVHTGERPYKCEECGKVFSWSSYLQAHQRVHTGEKPYKCEECGKGFSWSSSLIIHQRVHADDEGDKDFPSSEDSHRKTR
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
31SumoylationLLDLAQRKLYRDVML
HHHHHHHHHHHHHHH		37.48-
31SumoylationLLDLAQRKLYRDVML
HHHHHHHHHHHHHHH		37.48-
81UbiquitinationRDNSSGAKNLKEMET
CCCCCCCCCHHHHHH		67.3521890473
117SumoylationQITRELIKYQDSVVN
HHHHHHHHCHHHHEE		49.86-
117SumoylationQITRELIKYQDSVVN
HHHHHHHHCHHHHEE		49.8628112733
117UbiquitinationQITRELIKYQDSVVN
HHHHHHHHCHHHHEE		49.8621890473
159PhosphorylationLQVHRVHTGEKPYKG
EEEEEEECCCCCCCC		44.1529496963
162UbiquitinationHRVHTGEKPYKGEHC
EEEECCCCCCCCCCE		55.80-
162SumoylationHRVHTGEKPYKGEHC
EEEECCCCCCCCCCE		55.80-
162SumoylationHRVHTGEKPYKGEHC
EEEECCCCCCCCCCE		55.80-
206PhosphorylationNAFRRFSSLQAHQRV
HHHHHHHHHHHHHHH		23.0728555341
218MethylationQRVHSRAKSYTNDAS
HHHHHHHHHCCCCCH		42.77115978223
249SumoylationPTGENPYKYEECGRN
CCCCCCCCHHHCCCC		47.6628112733
271PhosphorylationQAPLIVHTGEKPYKC
CCCEEEEECCCCEEC		35.8229496963
274SumoylationLIVHTGEKPYKCEEC
EEEEECCCCEECCCC		55.80-
274UbiquitinationLIVHTGEKPYKCEEC
EEEEECCCCEECCCC		55.80-
274SumoylationLIVHTGEKPYKCEEC
EEEEECCCCEECCCC		55.80-
277SumoylationHTGEKPYKCEECGVG
EECCCCEECCCCCCC		43.63-
277SumoylationHTGEKPYKCEECGVG
EECCCCEECCCCCCC		43.63-
305SumoylationHTGKKPYKCEECGKS
ECCCCCEECCCCCCC		43.63-
305UbiquitinationHTGKKPYKCEECGKS
ECCCCCEECCCCCCC		43.63-
305SumoylationHTGKKPYKCEECGKS
ECCCCCEECCCCCCC		43.63-
327PhosphorylationQAHERIHTGEKPYKC
HHHCHHCCCCCCEEC		44.6729496963
355PhosphorylationNIHCRIHTGEKPYKC
EEEEEEECCCCCEEC		44.6729496963
358UbiquitinationCRIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
360PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
361UbiquitinationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
361SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
361SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
383PhosphorylationQAHQISHTGEKPYKC
EEEECCCCCCCCEEC		40.0024719451
389UbiquitinationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
389SumoylationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
389SumoylationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
429PhosphorylationGKGFSRSSDFNIHFR
CCCCCCCCCEEEEEE		45.1528555341
439PhosphorylationNIHFRVHTGEKPYKC
EEEEEEECCCCCEEC		44.1529496963
442UbiquitinationFRVHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
442SumoylationFRVHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
442SumoylationFRVHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
444PhosphorylationVHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
445UbiquitinationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
445SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
445SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
495PhosphorylationNVHCRIHTGEKPYKC
CEEEEEECCCCCCCC		44.6729496963
523PhosphorylationQVHQRVHTGEKPYQC
CEECCCCCCCCCEEE		44.15-
579PhosphorylationLAHRGVHTGEKPYRC
HHCCCCCCCCCCEEC		44.63-
582AcetylationRGVHTGEKPYRCDVC
CCCCCCCCCEECCCC		49.017695183
582UbiquitinationRGVHTGEKPYRCDVC
CCCCCCCCCEECCCC		49.01-
591AcetylationYRCDVCGKRFRQRSY
EECCCCCHHHHHHHH		43.147695191
607PhosphorylationQAHQRVHTGERPYKC
HHHCCHHCCCCCEEC		37.5727251275
613SumoylationHTGERPYKCEECGKV
HCCCCCEECCCCCCE		37.54-
613UbiquitinationHTGERPYKCEECGKV
HCCCCCEECCCCCCE		37.54-
613SumoylationHTGERPYKCEECGKV
HCCCCCEECCCCCCE		37.54-
635PhosphorylationQAHQRVHTGEKPYKC
HHHHHHHCCCCCEEC		44.1529496963
638SumoylationQRVHTGEKPYKCEEC
HHHHCCCCCEECCCC		55.80-
638UbiquitinationQRVHTGEKPYKCEEC
HHHHCCCCCEECCCC		55.80-
638SumoylationQRVHTGEKPYKCEEC
HHHHCCCCCEECCCC		55.80-
640PhosphorylationVHTGEKPYKCEECGK
HHCCCCCEECCCCCC		39.06-
641UbiquitinationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC		43.63-
641SumoylationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC		43.63-
641SumoylationHTGEKPYKCEECGKG
HCCCCCEECCCCCCC		43.63-
652PhosphorylationCGKGFSWSSSLIIHQ
CCCCCCCCCEEEEEE		14.6223186163
653PhosphorylationGKGFSWSSSLIIHQR
CCCCCCCCEEEEEEE		23.9423186163
654PhosphorylationKGFSWSSSLIIHQRV
CCCCCCCEEEEEEEE		20.3325106551
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 ZNF45_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF45_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 ZNF45_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF45_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 ZNF45_HUMAN

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Related Literatures of Post-Translational Modification

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