ZN420_HUMAN - dbPTM
ZN420_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN420_HUMAN
UniProt AC Q8TAQ5
Protein Name Zinc finger protein 420
Gene Name ZNF420
Organism Homo sapiens (Human).
Sequence Length 688
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MARKLVMFRDVAIDFSQEEWECLDSAQRDLYRDVMLENYSNLVSLDLPSRCASKDLSPEKNTYETELSQWEMSDRLENCDLEESNSRDYLEAKGKMEKQQENQKEYFRQGMIIYDKMSIFNQHTYLSQHSRCHSTEKPYKCKECGKAFRRASHLTQHQSIHTGEKPYECKQCGKAFSRDSQLSLHQRLHTGEKPYACKECGKAFTQSSQLILHHRIHTGEKPYKCEECGKAFIRSSQLTRHQKVHTGEKPYECKECGKAFTQNSQLTLHQRLHTGEKLYECKECRKVFTQLSQLILHKRIHTGEKPYECKECGKAFICGSQLSQHQKIHNGEKPYECKECGRAFIRGSLLMQHQRIHTGEKPYKCEECGKAFIRGSQLTQHQRIHTNEKPYECKECGKMFSHGSQLTQHQRIHTGEKPYQCKECGKAFNRGSLLTRHQRIHTGEKPYECKECGKTFSRGSELTQHERIHTGEKPYECKECGKSFIRGSQLTQHQRIHTGEKPYECKECRMAFTQSSHLSQHQRLHTGEKPYVCNECGKAFARGLLLIQHQRIHTGEKPYQCKECGKAFIRGSQLTQHQRIHTGEKPYECKECGKAFSHGSQLTLHQRIHTGEKPYECRECRKAFTQSSHLSRHQRIHTGEKPYQCKECGKAFTRGSQLTQHQRIHISEKSFEYKECGIDFSHGSQVYM
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
39PhosphorylationRDVMLENYSNLVSLD
HHHHCCCCCCCEECC		6.9119835603
40PhosphorylationDVMLENYSNLVSLDL
HHHCCCCCCCEECCC		34.9619835603
44PhosphorylationENYSNLVSLDLPSRC
CCCCCCEECCCCCHH		21.2329083192
49PhosphorylationLVSLDLPSRCASKDL
CEECCCCCHHHCCCC		47.4929083192
68PhosphorylationNTYETELSQWEMSDR
CCCHHHHHHHHHHHH		27.3222817900
150UbiquitinationECGKAFRRASHLTQH
HHHHHHHHHHHHHCC		33.7122505724
162PhosphorylationTQHQSIHTGEKPYEC
HCCCCCCCCCCCCCC		45.4229496963
170SumoylationGEKPYECKQCGKAFS
CCCCCCCCCCCCCCC		36.36-
170SumoylationGEKPYECKQCGKAFS
CCCCCCCCCCCCCCC		36.36-
190PhosphorylationSLHQRLHTGEKPYAC
CHHHHHHCCCCCCCH		52.1821857030
198UbiquitinationGEKPYACKECGKAFT
CCCCCCHHHHHCCCH		48.11-
218PhosphorylationILHHRIHTGEKPYKC
HEECCCCCCCCCEEC		44.6729496963
221UbiquitinationHRIHTGEKPYKCEEC
CCCCCCCCCEECHHH		55.80-
223PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHHHH		39.06-
224UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
224SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
224SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHH		43.63-
230UbiquitinationYKCEECGKAFIRSSQ
EECHHHHHHHHHHHH		52.35-
236PhosphorylationGKAFIRSSQLTRHQK
HHHHHHHHHCCCCCC		21.2528348404
246PhosphorylationTRHQKVHTGEKPYEC
CCCCCCCCCCCCCCC		50.4521857030
249UbiquitinationQKVHTGEKPYECKEC
CCCCCCCCCCCCCCC		55.00-
254SumoylationGEKPYECKECGKAFT
CCCCCCCCCCCCCCC		44.06-
254SumoylationGEKPYECKECGKAFT
CCCCCCCCCCCCCCC		44.06-
274PhosphorylationTLHQRLHTGEKLYEC
EEEHHHHCCCCCCCC		52.1821857030
290UbiquitinationECRKVFTQLSQLILH
HHHHHHHHHHHHHHH		27.8722505724
298SumoylationLSQLILHKRIHTGEK
HHHHHHHCCCCCCCC		49.9928112733
302PhosphorylationILHKRIHTGEKPYEC
HHHCCCCCCCCCCCC		44.6729496963
310SumoylationGEKPYECKECGKAFI
CCCCCCCCCCCCEEE		44.06-
310SumoylationGEKPYECKECGKAFI
CCCCCCCCCCCCEEE		44.06-
358PhosphorylationMQHQRIHTGEKPYKC
HHCCCCCCCCCCCCC		44.6729496963
361UbiquitinationQRIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		55.80-
363PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCCHHHCC		39.06-
364UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCCHHHCCE		43.63-
364SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHCCE		43.63-
364SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHCCE		43.63-
370UbiquitinationYKCEECGKAFIRGSQ
CCCHHHCCEEECCCC		52.35-
376PhosphorylationGKAFIRGSQLTQHQR
CCEEECCCCCCCCCC		16.50-
394SumoylationNEKPYECKECGKMFS
CCCCCCCCCHHCCCC		44.06-
394SumoylationNEKPYECKECGKMFS
CCCCCCCCCHHCCCC		44.06-
401PhosphorylationKECGKMFSHGSQLTQ
CCHHCCCCCHHHCCC		24.3629888752
404PhosphorylationGKMFSHGSQLTQHQR
HCCCCCHHHCCCCCC		19.3229888752
407PhosphorylationFSHGSQLTQHQRIHT
CCCHHHCCCCCCCCC		19.1729888752
414PhosphorylationTQHQRIHTGEKPYQC
CCCCCCCCCCCCCCC		44.6729888752
422UbiquitinationGEKPYQCKECGKAFN
CCCCCCCCCHHHCCC		40.28-
426AcetylationYQCKECGKAFNRGSL
CCCCCHHHCCCCCCC		62.5630593737
432PhosphorylationGKAFNRGSLLTRHQR
HHCCCCCCCHHHHCC		19.5724719451
442PhosphorylationTRHQRIHTGEKPYEC
HHHCCCCCCCCCCCC		44.6729496963
450SumoylationGEKPYECKECGKTFS
CCCCCCCCCCCCCCC		44.06-
450SumoylationGEKPYECKECGKTFS
CCCCCCCCCCCCCCC		44.06-
470PhosphorylationTQHERIHTGEKPYEC
CCCCCCCCCCCCCCC		44.6729496963
478SumoylationGEKPYECKECGKSFI
CCCCCCCCCCCCCEE		44.06-
478SumoylationGEKPYECKECGKSFI
CCCCCCCCCCCCCEE		44.06-
488PhosphorylationGKSFIRGSQLTQHQR
CCCEECCCCCCCCCE		16.5017525332
498PhosphorylationTQHQRIHTGEKPYEC
CCCCEECCCCCCCCC		44.6729496963
526PhosphorylationSQHQRLHTGEKPYVC
CHHCCCCCCCCCCCC		52.1821857030
529SumoylationQRLHTGEKPYVCNEC
CCCCCCCCCCCCCHH		42.89-
529SumoylationQRLHTGEKPYVCNEC
CCCCCCCCCCCCCHH		42.89-
554PhosphorylationIQHQRIHTGEKPYQC
EECCCCCCCCCCCCC		44.6728111955
562UbiquitinationGEKPYQCKECGKAFI
CCCCCCCCCCCCEEE		40.28-
566UbiquitinationYQCKECGKAFIRGSQ
CCCCCCCCEEECCCC		52.35-
572PhosphorylationGKAFIRGSQLTQHQR
CCEEECCCCCCCCCC		16.50-
582PhosphorylationTQHQRIHTGEKPYEC
CCCCCCCCCCCCCCC		44.6729496963
590SumoylationGEKPYECKECGKAFS
CCCCCCCCCCCCCCC		44.06-
590SumoylationGEKPYECKECGKAFS
CCCCCCCCCCCCCCC		44.06-
610PhosphorylationTLHQRIHTGEKPYEC
EEEECCCCCCCCCCH		44.6728111955
622SumoylationYECRECRKAFTQSSH
CCHHHHHHHHHCCHH		60.55-
622SumoylationYECRECRKAFTQSSH
CCHHHHHHHHHCCHH		60.55-
638PhosphorylationSRHQRIHTGEKPYQC
HHHCCCCCCCCCCCC		44.6728111955
646UbiquitinationGEKPYQCKECGKAFT
CCCCCCCCCCCCCCC		40.28-
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
68SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN420_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 ZN420_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
19377469
P53_HUMANTP53physical
20713054
CDN2A_HUMANCDKN2Aphysical
20713054
ARF_HUMANCDKN2Aphysical
20713054
MDM2_HUMANMDM2physical
25691462
CDN2A_HUMANCDKN2Aphysical
25691462
ARF_HUMANCDKN2Aphysical
25691462
UBC9_HUMANUBE2Iphysical
25691462
SENP1_HUMANSENP1physical
25691462
SAV1_HUMANSAV1physical
28514442
STK3_HUMANSTK3physical
28514442
H2AX_HUMANH2AFXphysical
28514442
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 ZN420_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY.

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