ZF64A_HUMAN - dbPTM
ZF64A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZF64A_HUMAN
UniProt AC Q9NPA5
Protein Name Zinc finger protein 64 homolog, isoforms 1 and 2
Gene Name ZFP64
Organism Homo sapiens (Human).
Sequence Length 681
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNASSEGESFAGSVQIPGGTTVLVELTPDIHICGICKQQFNNLDAFVAHKQSGCQLTGTSAAAPSTVQFVSEETVPATQTQTTTRTITSETQTITVSAPEFVFEHGYQTYLPTESNENQTATVISLPAKSRTKKPTTPPAQKRLNCCYPGCQFKTAYGMKDMERHLKIHTGDKPHKCEVCGKCFSRKDKLKTHMRCHTGVKPYKCKTCDYAAADSSSLNKHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHTGDAPFQCWLCSAKFKISSDLKRHMRVHSGEKPFKCEFCNVRCTMKGNLKSHIRIKHSGNNFKCPHCDFLGDSKATLRKHSRVHQSEHPEKCSECSYSCSSKAALRIHERIHCTDRPFKCNYCSFDTKQPSNLSKHMKKFHGDMVKTEALERKDTGRQSSRQVAKLDAKKSFHCDICDASFMREDSLRSHKRQHSEYSESKNSDVTVLQFQIDPSKQPATPLTVGHLQVPLQPSQVPQFSEGRVKIIVGHQVPQANTIVQAAAAAVNIVPPALVAQNPEELPGNSRLQILRQVSLIAPPQSSRCPSEAGAMTQPAVLLTTHEQTDGATLHQTLIPTASGGPQEGSGNQTFITSSGITCTDFEGLNALIQEGTAEVTVVSDGGQNIAVATTAPPVFSSSSQQELPKQTYSIIQGAAHPALLCPADSIPD
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
142AcetylationPTTPPAQKRLNCCYP
CCCCHHHHHCCCCCC
62.0424431651
232MethylationHSDERPFKCQICPYA
CCCCCCEEEEECCCC
28.10115978315
288SumoylationHSGEKPFKCEFCNVR
CCCCCCEECEECCCE
41.1928112733
399SumoylationKFHGDMVKTEALERK
HHCCHHHHHHHHHCC
33.7328112733

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 ZF64A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZF64A_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 ZF64A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BEGIN_HUMANBEGAINphysical
16189514
ERG28_HUMANC14orf1physical
16169070
SETB1_HUMANSETDB1physical
16169070
U119A_HUMANUNC119physical
16169070
TLE1_HUMANTLE1physical
16169070
ZN513_HUMANZNF513physical
20211142
PRGC2_HUMANPPARGC1Bphysical
20211142
ZBTB9_HUMANZBTB9physical
20211142
TOPK_HUMANPBKphysical
25416956
AEN_HUMANAENphysical
25416956
LNX1_HUMANLNX1physical
25416956
TRI41_HUMANTRIM41physical
25416956
F124A_HUMANFAM124Aphysical
25416956
AEN_HUMANAENphysical
21516116
TRI41_HUMANTRIM41physical
21516116

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 ZF64A_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 THR-473 AND SER-487, ANDMASS SPECTROMETRY.

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