ZN708_HUMAN - dbPTM
ZN708_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN708_HUMAN
UniProt AC P17019
Protein Name Zinc finger protein 708
Gene Name ZNF708
Organism Homo sapiens (Human).
Sequence Length 499
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MKRHEMAAKPPAMCSHFAKDLRPEQYIKNSFQQVILRRYGKCGYQKGCKSVDEHKLHKGGHKGLNRCVTTTQSKIVQCDKYVKVFHKYSNAKRHKIRHTGKNPFKCKECGKSFCMLSQLTQHEIIHTGEKPYKCEECGKAFKKSSNLTNHKIIHTGEKPYKCEECGKAFNQSSTLTRHKIIHTGEKLYKCEECGKAFNRSSNLTKHKIVHTGEKPYKCEECGKAFKQSSNLTNHKKIHTGEKPYKCGECGKAFTLSSHLTTHKRIHTGEKPYKCEECGKAFSVFSTLTKHKIIHTEEKPYKCEECGKAFNRSSHLTNHKVIHTGEKPYKCEECGKAFTKSSTLTYHKVIHTGKKPYKCEECGKAFSIFSILTKHKVIHTEDKPYKCEECGKTFNYSSNFTNHKKIHTGEKPYKCEECGKSFILSSHLTTHKIIHTGEKPYKCKECGKAFNQSSTLMKHKIIHTGEKPYKCEECGKAFNQSPNLTKHKRIHTKEKPYKCK
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
50PhosphorylationGYQKGCKSVDEHKLH
CCCCCCCCCCCCCCC		4.4029485707
69O-linked_GlycosylationKGLNRCVTTTQSKIV
CCCCCCEECCHHHHE		34.2530379171
83UbiquitinationVQCDKYVKVFHKYSN
EECHHHHHHHHHHCC		57.25-
99PhosphorylationKRHKIRHTGKNPFKC
CCCCCCCCCCCCCCC		1.84-
127PhosphorylationTQHEIIHTGEKPYKC
HCCCCCCCCCCCCCH		23.6229496963
130UbiquitinationEIIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		22.71-
132PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		4.87-
133AcetylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		27.9619825549
133SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		27.96-
133UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		27.96-
133SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		27.96-
151UbiquitinationSSNLTNHKIIHTGEK
HCCCCCCCEEECCCC		38.62-
155PhosphorylationTNHKIIHTGEKPYKC
CCCCEEECCCCCEEC		12.3429496963
158UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEECHHH		29.23-
160PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECHHHHH		2.97-
161AcetylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		26.5619825555
161SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		26.56-
161UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		26.56-
161SumoylationHTGEKPYKCEECGKA
ECCCCCEECHHHHHC		26.56-
167UbiquitinationYKCEECGKAFNQSST
EECHHHHHCCCCCCC		33.29-
167AcetylationYKCEECGKAFNQSST
EECHHHHHCCCCCCC		33.2920167786
183PhosphorylationTRHKIIHTGEKLYKC
CCEEEEECCCCEEEH		4.4627251275
183UbiquitinationTRHKIIHTGEKLYKC
CCEEEEECCCCEEEH		4.4622505724
188PhosphorylationIHTGEKLYKCEECGK
EECCCCEEEHHHHHH		2.34-
189SumoylationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHC		1.85-
189SumoylationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHC		1.85-
189UbiquitinationHTGEKLYKCEECGKA
ECCCCEEEHHHHHHC		1.85-
195UbiquitinationYKCEECGKAFNRSSN
EEHHHHHHCCCCCCC		29.5222505724
211PhosphorylationTKHKIVHTGEKPYKC
CCCCEEECCCCCEEH		5.6829496963
214SumoylationKIVHTGEKPYKCEEC
CEEECCCCCEEHHHH		19.91-
214SumoylationKIVHTGEKPYKCEEC
CEEECCCCCEEHHHH		19.91-
214UbiquitinationKIVHTGEKPYKCEEC
CEEECCCCCEEHHHH		19.91-
216PhosphorylationVHTGEKPYKCEECGK
EECCCCCEEHHHHHH		1.86-
217SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		2.58-
217SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		2.58-
217UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		2.58-
232PhosphorylationFKQSSNLTNHKKIHT
HHHHCCCCCCCCEEC		8.23-
236UbiquitinationSNLTNHKKIHTGEKP
CCCCCCCCEECCCCC		26.79-
239PhosphorylationTNHKKIHTGEKPYKC
CCCCCEECCCCCEEC		4.2429496963
245SumoylationHTGEKPYKCGECGKA
ECCCCCEECCCCCCE		2.58-
245SumoylationHTGEKPYKCGECGKA
ECCCCCEECCCCCCE		2.58-
253UbiquitinationCGECGKAFTLSSHLT
CCCCCCEEEEHHCHH		45.6822505724
259UbiquitinationAFTLSSHLTTHKRIH
EEEEHHCHHCCCCCC		62.5622505724
261PhosphorylationTLSSHLTTHKRIHTG
EEHHCHHCCCCCCCC		9.9524719451
267PhosphorylationTTHKRIHTGEKPYKC
HCCCCCCCCCCCEEC		7.9329496963
270UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECCCC		21.60-
272PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECCCCCC		2.48-
273SumoylationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		3.84-
273UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		3.84-
273SumoylationHTGEKPYKCEECGKA
CCCCCCEECCCCCCC		3.84-
282PhosphorylationEECGKAFSVFSTLTK
CCCCCCHHHHHHHHC		4.3719413330
289UbiquitinationSVFSTLTKHKIIHTE
HHHHHHHCCCEEECC		9.36-
295UbiquitinationTKHKIIHTEEKPYKC
HCCCEEECCCCCCCH		5.6822505724
298SumoylationKIIHTEEKPYKCEEC
CEEECCCCCCCHHHH		27.79-
298SumoylationKIIHTEEKPYKCEEC
CEEECCCCCCCHHHH		27.79-
301SumoylationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHC		4.13-
301SumoylationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHC		4.13-
301UbiquitinationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHC		4.13-
307UbiquitinationYKCEECGKAFNRSSH
CCHHHHHHCCCCCCC		29.5222505724
323PhosphorylationTNHKVIHTGEKPYKC
CCCCEEECCCCCEEC		6.8029496963
326UbiquitinationKVIHTGEKPYKCEEC
CEEECCCCCEECCCC		16.50-
328PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		20.51-
329AcetylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		3.9830593891
329SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		3.98-
329UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		3.98-
329SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		3.98-
351PhosphorylationTYHKVIHTGKKPYKC
EEEEEEECCCCCEEC		6.10-
357SumoylationHTGKKPYKCEECGKA
ECCCCCEECCHHCCC		3.81-
357SumoylationHTGKKPYKCEECGKA
ECCCCCEECCHHCCC		3.81-
357UbiquitinationHTGKKPYKCEECGKA
ECCCCCEECCHHCCC		3.81-
363AcetylationYKCEECGKAFSIFSI
EECCHHCCCHHHHHH		36.787926707
365UbiquitinationCEECGKAFSIFSILT
CCHHCCCHHHHHHHH		43.6322505724
366O-linked_GlycosylationEECGKAFSIFSILTK
CHHCCCHHHHHHHHC		4.3730379171
369PhosphorylationGKAFSIFSILTKHKV
CCCHHHHHHHHCCCE		2.9424719451
371UbiquitinationAFSIFSILTKHKVIH
CHHHHHHHHCCCEEE		62.5622505724
373UbiquitinationSIFSILTKHKVIHTE
HHHHHHHCCCEEECC		9.9527667366
375AcetylationFSILTKHKVIHTEDK
HHHHHCCCEEECCCC		32.847926715
382AcetylationKVIHTEDKPYKCEEC
CEEECCCCCEECHHC		22.117926723
385SumoylationHTEDKPYKCEECGKT
ECCCCCEECHHCCCE		2.61-
385SumoylationHTEDKPYKCEECGKT
ECCCCCEECHHCCCE		2.61-
385UbiquitinationHTEDKPYKCEECGKT
ECCCCCEECHHCCCE		2.6127667366
404UbiquitinationSNFTNHKKIHTGEKP
CCCCCCCEEECCCCC		26.04-
407PhosphorylationTNHKKIHTGEKPYKC
CCCCEEECCCCCEEC		4.9029496963
410UbiquitinationKKIHTGEKPYKCEEC
CEEECCCCCEECCCC		16.81-
412PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		2.18-
413SumoylationHTGEKPYKCEECGKS
ECCCCCEECCCCCCE		2.61-
413UbiquitinationHTGEKPYKCEECGKS
ECCCCCEECCCCCCE		2.61-
413SumoylationHTGEKPYKCEECGKS
ECCCCCEECCCCCCE		2.61-
431UbiquitinationSSHLTTHKIIHTGEK
ECCCCCCEEEECCCC		2.25-
435PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCCCC		5.1729496963
438UbiquitinationKIIHTGEKPYKCKEC
EEEECCCCCCCCCHH		25.12-
440PhosphorylationIHTGEKPYKCKECGK
EECCCCCCCCCHHHH		3.76-
443UbiquitinationGEKPYKCKECGKAFN
CCCCCCCCHHHHCCC		34.4527667366
449UbiquitinationCKECGKAFNQSSTLM
CCHHHHCCCCCHHHH		43.6327667366
459UbiquitinationSSTLMKHKIIHTGEK
CHHHHHCCEEECCCC		14.86-
463PhosphorylationMKHKIIHTGEKPYKC
HHCCEEECCCCCEEH		8.5929496963
466UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEEHHHH		29.72-
468PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		31.97-
469AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		4.1319825561
469SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		4.13-
469UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		4.13-
469SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		4.13-
480PhosphorylationCGKAFNQSPNLTKHK
HHHHHCCCCCCCCCC		59.0225849741
544Phosphorylation----------------------------------------------------
----------------------------------------------------		19.5021406692
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 ZN708_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN708_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 ZN708_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN708_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 ZN708_HUMAN

loading...

Related Literatures of Post-Translational Modification

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