ZN576_HUMAN - dbPTM
ZN576_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN576_HUMAN
UniProt AC Q9H609
Protein Name Zinc finger protein 576
Gene Name ZNF576
Organism Homo sapiens (Human).
Sequence Length 170
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEDPNPEENMKQQDSPKERSPQSPGGNICHLGAPKCTRCLITFADSKFQERHMKREHPADFVAQKLQGVLFICFTCARSFPSSKALITHQRSHGPAAKPTLPVATTTAQPTFPCPDCGKTFGQAVSLRRHRQMHEVRAPPGTFACTECGQDFAQEAGLHQHYIRHARGEL
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
15PhosphorylationENMKQQDSPKERSPQ
HHHCCCCCCCCCCCC
33.2724719451
20PhosphorylationQDSPKERSPQSPGGN
CCCCCCCCCCCCCCC
28.5125159151
23PhosphorylationPKERSPQSPGGNICH
CCCCCCCCCCCCCCC
28.9725159151
75PhosphorylationGVLFICFTCARSFPS
HHHHHHHHCCCCCCC
10.8025404012
79PhosphorylationICFTCARSFPSSKAL
HHHHCCCCCCCCHHH
24.0028060719
82PhosphorylationTCARSFPSSKALITH
HCCCCCCCCHHHHHC
42.3228060719
83PhosphorylationCARSFPSSKALITHQ
CCCCCCCCHHHHHCH
23.3728060719
105PhosphorylationKPTLPVATTTAQPTF
CCCCCEEECCCCCCC
25.5530576142
107PhosphorylationTLPVATTTAQPTFPC
CCCEEECCCCCCCCC
20.95-
111PhosphorylationATTTAQPTFPCPDCG
EECCCCCCCCCCCCC
28.29-
120PhosphorylationPCPDCGKTFGQAVSL
CCCCCCCCHHHHHHH
20.4822817900
126PhosphorylationKTFGQAVSLRRHRQM
CCHHHHHHHHHHHHH
21.1222817900

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 ZN576_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN576_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 ZN576_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POGZ_HUMANPOGZphysical
28514442
ZN618_HUMANZNF618physical
28514442
AJUBA_HUMANAJUBAphysical
28514442
ZBT40_HUMANZBTB40physical
28514442
ZBED1_HUMANZBED1physical
28514442
ZBT10_HUMANZBTB10physical
28514442
LIMD1_HUMANLIMD1physical
28514442
RBBP6_HUMANRBBP6physical
28514442
PDLI7_HUMANPDLIM7physical
28514442
KAISO_HUMANZBTB33physical
28514442
ZN446_HUMANZNF446physical
28514442
RENT1_HUMANUPF1physical
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 ZN576_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120 AND SER-126, ANDMASS SPECTROMETRY.

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