ZN251_HUMAN - dbPTM
ZN251_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN251_HUMAN
UniProt AC Q9BRH9
Protein Name Zinc finger protein 251
Gene Name ZNF251
Organism Homo sapiens (Human).
Sequence Length 671
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAATFQLPGHQEMPLTFQDVAVYFSQAEGRQLGPQQRALYRDVMLENYGNVASLGFPVPKPELISQLEQGKELWVLNLLGAEEPDILKSCQKDSEVGTKKELSILNQKFSEEVKTPEFVSRRLLRDNAQAAEFREAWGREGKLKERVGNSAGQSLNKPNIHKRVLTEATVGRERSLGERTQECSAFDRNLNLDQNVVRLQRNKTGERVFKCDICSKTFKYNSDLSRHQRSHTGEKPYECGRCGRAFTHSSNLVLHHHIHTGNKPFKCDECGKTFGLNSHLRLHRRIHTGEKPFGCGECGKAFSRSSTLIQHRIIHTGEKPYKCNECGRGFSQSPQLTQHQRIHTGEKPHECSHCGKAFSRSSSLIQHERIHTGEKPHKCNQCGKAFSQSSSLFLHHRVHTGEKPYVCNECGRAFGFNSHLTEHVRIHTGEKPYVCNECGKAFRRSSTLVQHRRVHTGEKPYQCVECGKAFSQSSQLTLHQRVHTGEKPYDCGDCGKAFSRRSTLIQHQKVHSGETRKCRKHGPAFVHGSSLTADGQIPTGEKHGRAFNHGANLILRWTVHTGEKSFGCNEYGKAFSPTSRPTEDQIMHAGEKPYKCQECGNAFSGKSTLIQHQVTHTGQKPCHCSVYGKAFSQSSQLTPPQQTRVGEKPALNDGSKRYFIHIKKIFQERHF
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
23PhosphorylationTFQDVAVYFSQAEGR
EHHHEEEEEEHHHCC		6.4330576742
25PhosphorylationQDVAVYFSQAEGRQL
HHEEEEEEHHHCCCC		15.7030576742
100SumoylationDSEVGTKKELSILNQ
CCCCCCHHHHHHHHH		64.82-
100SumoylationDSEVGTKKELSILNQ
CCCCCCHHHHHHHHH		64.82-
103PhosphorylationVGTKKELSILNQKFS
CCCHHHHHHHHHHHC		26.5623532336
108UbiquitinationELSILNQKFSEEVKT
HHHHHHHHHCHHCCC		50.1929967540
114SumoylationQKFSEEVKTPEFVSR
HHHCHHCCCHHHHHH		62.74-
114UbiquitinationQKFSEEVKTPEFVSR
HHHCHHCCCHHHHHH		62.7429967540
114SumoylationQKFSEEVKTPEFVSR
HHHCHHCCCHHHHHH		62.7428112733
115PhosphorylationKFSEEVKTPEFVSRR
HHCHHCCCHHHHHHH		32.9728555341
154PhosphorylationVGNSAGQSLNKPNIH
HCCCCCCCCCCCCHH		32.7528555341
157SumoylationSAGQSLNKPNIHKRV
CCCCCCCCCCHHHHH		44.74-
157SumoylationSAGQSLNKPNIHKRV
CCCCCCCCCCHHHHH		44.7428112733
162SumoylationLNKPNIHKRVLTEAT
CCCCCHHHHHHHHHH		40.1728112733
180PhosphorylationERSLGERTQECSAFD
CCCHHHHHHHCCHHH		25.15-
184PhosphorylationGERTQECSAFDRNLN
HHHHHHCCHHHCCCC		31.08-
210SumoylationKTGERVFKCDICSKT
CCCCEEEECCCCCCE		28.30-
210SumoylationKTGERVFKCDICSKT
CCCCEEEECCCCCCE		28.30-
247PhosphorylationGRCGRAFTHSSNLVL
CCCCCCCCCCCCEEE		21.62-
249PhosphorylationCGRAFTHSSNLVLHH
CCCCCCCCCCEEEEE		20.19-
250PhosphorylationGRAFTHSSNLVLHHH
CCCCCCCCCEEEEEE		26.95-
278PhosphorylationGKTFGLNSHLRLHRR
CCCCCCCHHHHHHHC		29.01-
300SumoylationFGCGECGKAFSRSST
CCCCCCCCCCCCCCC		58.90-
300SumoylationFGCGECGKAFSRSST
CCCCCCCCCCCCCCC		58.90-
316PhosphorylationIQHRIIHTGEKPYKC
EEEEEEECCCCCEEC		36.3129496963
319UbiquitinationRIIHTGEKPYKCNEC
EEEECCCCCEECCCC		55.80-
333PhosphorylationCGRGFSQSPQLTQHQ
CCCCCCCCCCCCCCC		17.2625159151
362PhosphorylationGKAFSRSSSLIQHER
CCCCCCCCCHHHHCC		28.2227251275
363PhosphorylationKAFSRSSSLIQHERI
CCCCCCCCHHHHCCC		30.6428555341
400PhosphorylationFLHHRVHTGEKPYVC
EEEEEECCCCCCEEE		44.15-
403SumoylationHRVHTGEKPYVCNEC
EEECCCCCCEEECCC		42.8928112733
403SumoylationHRVHTGEKPYVCNEC
EEECCCCCCEEECCC		42.89-
428PhosphorylationTEHVRIHTGEKPYVC
CCCEEEECCCCCEEE		44.6728111955
456PhosphorylationVQHRRVHTGEKPYQC
HCCCCCCCCCCCEEE		44.15-
484PhosphorylationTLHQRVHTGEKPYDC
EEEEEECCCCCCCCC		44.15-
487UbiquitinationQRVHTGEKPYDCGDC
EEECCCCCCCCCCCC		50.66-
496SumoylationYDCGDCGKAFSRRST
CCCCCCCHHCCCCCH		53.22-
496SumoylationYDCGDCGKAFSRRST
CCCCCCCHHCCCCCH		53.22-
520UbiquitinationGETRKCRKHGPAFVH
CCCCHHHCCCCCEEE		63.4829967540
522PhosphorylationTRKCRKHGPAFVHGS
CCHHHCCCCCEEECC		20.4715302935
565PhosphorylationTVHTGEKSFGCNEYG
EEECCCCCCCCCCCC		23.6722817900
576PhosphorylationNEYGKAFSPTSRPTE
CCCCCCCCCCCCCCH		31.9325159151
582PhosphorylationFSPTSRPTEDQIMHA
CCCCCCCCHHHHCCC		51.5922210691
595SumoylationHAGEKPYKCQECGNA
CCCCCCCCCCCCCCC		37.66-
595SumoylationHAGEKPYKCQECGNA
CCCCCCCCCCCCCCC		37.66-
648UbiquitinationQQTRVGEKPALNDGS
CCCCCCCCCCCCCCC		29.6629967540
648SumoylationQQTRVGEKPALNDGS
CCCCCCCCCCCCCCC		29.66-
648SumoylationQQTRVGEKPALNDGS
CCCCCCCCCCCCCCC		29.66-
658PhosphorylationLNDGSKRYFIHIKKI
CCCCCCEEEEEEHHH		15.60-
664SumoylationRYFIHIKKIFQERHF
EEEEEEHHHHHHCCC		48.42-
664SumoylationRYFIHIKKIFQERHF
EEEEEEHHHHHHCCC		48.42-
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 ZN251_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN251_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 ZN251_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN251_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 ZN251_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory