ZN300_HUMAN - dbPTM
ZN300_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN300_HUMAN
UniProt AC Q96RE9
Protein Name Zinc finger protein 300
Gene Name ZNF300
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Nucleus .
Protein Description Has a transcriptional repressor activity..
Protein Sequence MMKSQGLVSFKDVAVDFTQEEWQQLDPSQRTLYRDVMLENYSHLVSMGYPVSKPDVISKLEQGEEPWIIKGDISNWIYPDEYQADGRQDRKSNLHNSQSCILGTVSFHHKILKGVTRDGSLCSILKVCQGDGQLQRFLENQDKLFRQVTFVNSKTVTEASGHKYNPLGKIFQECIETDISIQRFHKYDAFKKNLKPNIDLPSCYKSNSRKKPDQSFGGGKSSSQSEPNSNLEKIHNGVIPFDDNQCGNVFRNTQSLIQYQNVETKEKSCVCVTCGKAFAKKSQLIVHQRIHTGKKPYDCGACGKAFSEKFHLVVHQRTHTGEKPYDCSECGKAFSQKSSLIIHQRVHTGEKPYECSECGKAFSQKSPLIIHQRIHTGEKPYECRECGKAFSQKSQLIIHHRAHTGEKPYECTECGKAFCEKSHLIIHKRIHTGEKPYKCAQCEEAFSRKTELITHQLVHTGEKPYECTECGKTFSRKSQLIIHQRTHTGEKPYKCSECGKAFCQKSHLIGHQRIHTGEKPYICTECGKAFSQKSHLPGHQRIHTGEKPYICAECGKAFSQKSDLVLHQRIHTGERPYQCAICGKAFIQKSQLTVHQRIHTVVKS
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
9 (in isoform 3)Phosphorylation-31.46-
9 (in isoform 2)Phosphorylation-31.46-
41PhosphorylationRDVMLENYSHLVSMG
HHHHHHCHHHHHHCC		6.5225072903
42PhosphorylationDVMLENYSHLVSMGY
HHHHHCHHHHHHCCC		23.1725072903
46PhosphorylationENYSHLVSMGYPVSK
HCHHHHHHCCCCCCC		16.9225072903
49PhosphorylationSHLVSMGYPVSKPDV
HHHHHCCCCCCCHHH		7.5725072903
52PhosphorylationVSMGYPVSKPDVISK
HHCCCCCCCHHHHHH		33.6925072903
58PhosphorylationVSKPDVISKLEQGEE
CCCHHHHHHHHCCCC		30.9125072903
92PhosphorylationDGRQDRKSNLHNSQS
CCCCCHHHCCCCCCC		45.5821060948
97PhosphorylationRKSNLHNSQSCILGT
HHHCCCCCCCCEEEH		16.8421060948
99PhosphorylationSNLHNSQSCILGTVS
HCCCCCCCCEEEHHH		11.7121060948
120PhosphorylationKGVTRDGSLCSILKV
CCCCCCCCCHHHEEE		30.4128060719
123PhosphorylationTRDGSLCSILKVCQG
CCCCCCHHHEEEECC		35.9324719451
164PhosphorylationTEASGHKYNPLGKIF
EECCCCCCCCHHHHH		19.15-
177PhosphorylationIFQECIETDISIQRF
HHHHHHHCCCCHHHH		20.79-
180PhosphorylationECIETDISIQRFHKY
HHHHCCCCHHHHHHH		18.58-
195SumoylationDAFKKNLKPNIDLPS
HHHHHCCCCCCCCCH		45.47-
195SumoylationDAFKKNLKPNIDLPS
HHHHHCCCCCCCCCH		45.47-
265SumoylationQYQNVETKEKSCVCV
HEECCCCCCCEEEEE		50.03-
265SumoylationQYQNVETKEKSCVCV
HEECCCCCCCEEEEE		50.03-
297PhosphorylationIHTGKKPYDCGACGK
ECCCCCCCCCCCCCH		32.51-
307PhosphorylationGACGKAFSEKFHLVV
CCCCHHHHHHEEEEE		44.7424719451
318PhosphorylationHLVVHQRTHTGEKPY
EEEEEECCCCCCCCC		19.74-
320PhosphorylationVVHQRTHTGEKPYDC
EEEECCCCCCCCCCH		46.56-
348PhosphorylationIIHQRVHTGEKPYEC
EEEEEEECCCCCEEC		44.1528348404
356PhosphorylationGEKPYECSECGKAFS
CCCCEECCCCCCCCC		24.79-
366PhosphorylationGKAFSQKSPLIIHQR
CCCCCCCCCEEEEEE		19.8028555341
376PhosphorylationIIHQRIHTGEKPYEC
EEEEEECCCCCCEEH		44.6728111955
391PhosphorylationRECGKAFSQKSQLII
HHHHHHHHHCCEEEE		41.3722199227
394PhosphorylationGKAFSQKSQLIIHHR
HHHHHHCCEEEEECC		23.6822777824
432PhosphorylationIIHKRIHTGEKPYKC
EEEEEEECCCCCCCC		44.6729496963
460PhosphorylationITHQLVHTGEKPYEC
HEEECCCCCCCCEEC		39.2920068231
477SumoylationCGKTFSRKSQLIIHQ
CCCEECCCCEEEEEE		41.16-
477SumoylationCGKTFSRKSQLIIHQ
CCCEECCCCEEEEEE		41.16-
486PhosphorylationQLIIHQRTHTGEKPY
EEEEEECCCCCCCCE		19.7428348404
488PhosphorylationIIHQRTHTGEKPYKC
EEEECCCCCCCCEEC		46.5624719451
491AcetylationQRTHTGEKPYKCSEC
ECCCCCCCCEECCHH		55.807428881
491UbiquitinationQRTHTGEKPYKCSEC
ECCCCCCCCEECCHH		55.80-
493PhosphorylationTHTGEKPYKCSECGK
CCCCCCCEECCHHHH		35.38-
496PhosphorylationGEKPYKCSECGKAFC
CCCCEECCHHHHHHH		31.59-
516PhosphorylationIGHQRIHTGEKPYIC
CCCCCCCCCCCCEEE		44.6728111955
519SumoylationQRIHTGEKPYICTEC
CCCCCCCCCEEECCC		44.45-
519SumoylationQRIHTGEKPYICTEC
CCCCCCCCCEEECCC		44.45-
521PhosphorylationIHTGEKPYICTECGK
CCCCCCCEEECCCCC		21.50-
544PhosphorylationPGHQRIHTGEKPYIC
CCCCCCCCCCCCEEE		44.6728111955
547SumoylationQRIHTGEKPYICAEC
CCCCCCCCCEEEECC		44.45-
547SumoylationQRIHTGEKPYICAEC
CCCCCCCCCEEEECC		44.45-
548UbiquitinationRIHTGEKPYICAECG
CCCCCCCCEEEECCC		21.3029967540
584UbiquitinationYQCAICGKAFIQKSQ
CEEEECCCEEEEHHC		35.3929967540
600UbiquitinationTVHQRIHTVVKS---
EHHHHHHHHCCC---		25.3229967540
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 ZN300_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN300_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 ZN300_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN300_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 ZN300_HUMAN

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Related Literatures of Post-Translational Modification

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