ZN248_HUMAN - dbPTM
ZN248_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN248_HUMAN
UniProt AC Q8NDW4
Protein Name Zinc finger protein 248
Gene Name ZNF248
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNKSQEQVSFKDVCVDFTQEEWYLLDPAQKILYRDVILENYSNLVSVGYCITKPEVIFKIEQGEEPWILEKGFPSQCHPERKWKVDDVLESSQENEDDHFWELLFHNNKTVSVENGDRGSKTFNLGTDPVSLRNYPYKICDSCEMNLKNISGLIISKKNCSRKKPDEFNVCEKLLLDIRHEKIPIGEKSYKYDQKRNAINYHQDLSQPSFGQSFEYSKNGQGFHDEAAFFTNKRSQIGETVCKYNECGRTFIESLKLNISQRPHLEMEPYGCSICGKSFCMNLRFGHQRALTKDNPYEYNEYGEIFCDNSAFIIHQGAYTRKILREYKVSDKTWEKSALLKHQIVHMGGKSYDYNENGSNFSKKSHLTQLRRAHTGEKTFECGECGKTFWEKSNLTQHQRTHTGEKPYECTECGKAFCQKPHLTNHQRTHTGEKPYECKQCGKTFCVKSNLTEHQRTHTGEKPYECNACGKSFCHRSALTVHQRTHTGEKPFICNECGKSFCVKSNLIVHQRTHTGEKPYKCNECGKTFCEKSALTKHQRTHTGEKPYECNACGKTFSQRSVLTKHQRIHTRVKALSTS
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
71UbiquitinationEEPWILEKGFPSQCH
CCCEEEECCCCCCCC		63.51-
121UbiquitinationENGDRGSKTFNLGTD
ECCCCCCCEEECCCC		61.02-
142PhosphorylationYPYKICDSCEMNLKN
CCHHHCCCCCCCCCC		13.9418187866
156PhosphorylationNISGLIISKKNCSRK
CCEEEEEECCCCCCC		30.50-
188UbiquitinationEKIPIGEKSYKYDQK
CCCCCCCCCCCHHHH		54.60-
243UbiquitinationQIGETVCKYNECGRT
HHCCCCCCCCCCCCH		46.93-
327PhosphorylationTRKILREYKVSDKTW
HHHHHHHCCCCCCCC		15.40-
330PhosphorylationILREYKVSDKTWEKS
HHHHCCCCCCCCCHH		29.27-
341SumoylationWEKSALLKHQIVHMG
CCHHHHHHEEEEECC		34.0228112733
341UbiquitinationWEKSALLKHQIVHMG
CCHHHHHHEEEEECC		34.02-
363SumoylationENGSNFSKKSHLTQL
CCCCCCCCHHHHHHH		54.91-
364SumoylationNGSNFSKKSHLTQLR
CCCCCCCHHHHHHHH		41.74-
401PhosphorylationNLTQHQRTHTGEKPY
CCCCCCCCCCCCCCE		19.74-
403PhosphorylationTQHQRTHTGEKPYEC
CCCCCCCCCCCCEEE		46.5624719451
408PhosphorylationTHTGEKPYECTECGK
CCCCCCCEEECCCHH		34.4024719451
411PhosphorylationGEKPYECTECGKAFC
CCCCEEECCCHHCHH		23.5224719451
429PhosphorylationHLTNHQRTHTGEKPY
CCCCCCCCCCCCCCE		19.7429396449
431PhosphorylationTNHQRTHTGEKPYEC
CCCCCCCCCCCCEEC		46.5629496963
434UbiquitinationQRTHTGEKPYECKQC
CCCCCCCCCEECCCC		55.00-
436PhosphorylationTHTGEKPYECKQCGK
CCCCCCCEECCCCCC		45.0530576142
439SumoylationGEKPYECKQCGKTFC
CCCCEECCCCCCEEE		36.36-
439SumoylationGEKPYECKQCGKTFC
CCCCEECCCCCCEEE		36.36-
444PhosphorylationECKQCGKTFCVKSNL
ECCCCCCEEEEECCC		13.9330576142
452PhosphorylationFCVKSNLTEHQRTHT
EEEECCCCCCCCCCC		35.3530576142
457PhosphorylationNLTEHQRTHTGEKPY
CCCCCCCCCCCCCCC		19.74-
459PhosphorylationTEHQRTHTGEKPYEC
CCCCCCCCCCCCCCC		46.56-
480PhosphorylationFCHRSALTVHQRTHT
CCCCCCCEEECCCCC		18.6923532336
485PhosphorylationALTVHQRTHTGEKPF
CCEEECCCCCCCCCE		19.74-
487PhosphorylationTVHQRTHTGEKPFIC
EEECCCCCCCCCEEE		46.56-
513PhosphorylationNLIVHQRTHTGEKPY
CEEEEECCCCCCCCE		19.7428348404
515PhosphorylationIVHQRTHTGEKPYKC
EEEECCCCCCCCEEC		46.5626270265
518UbiquitinationQRTHTGEKPYKCNEC
ECCCCCCCCEECCCC		55.80-
520PhosphorylationTHTGEKPYKCNECGK
CCCCCCCEECCCCCC		38.96-
521SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
521SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
541PhosphorylationALTKHQRTHTGEKPY
HCCCCCCCCCCCCCE		19.74-
543PhosphorylationTKHQRTHTGEKPYEC
CCCCCCCCCCCCEEC		46.56-
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 ZN248_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN248_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 ZN248_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN248_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 ZN248_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.

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