dbPTM

ZN589_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN589_HUMAN
UniProt AC	Q86UQ0
Protein Name	Zinc finger protein 589
Gene Name	ZNF589
Organism	Homo sapiens (Human).
Sequence Length	364
Subcellular Localization	Nucleus .
Protein Description	May play a role in hematopoietic stem/progenitor cell differentiation. May play a role as a DNA binding-dependent transcriptional repressor..
Protein Sequence	MWAPREQLLGWTAEALPAKDSAWPWEEKPRYLGPVTFEDVAVLFTEAEWKRLSLEQRNLYKEVMLENLRNLVSLAESKPEVHTCPSCPLAFGSQQFLSQDELHNHPIPGFHAGNQLHPGNPCPEDQPQSQHPSDKNHRGAEAEDQRVEGGVRPLFWSTNERGALVGFSSLFQRPPISSWGGNRILEIQLSPAQNASSEEVDRISKRAETPGFGAVTFGECALAFNQKSNLFRQKAVTAEKSSDKRQSQVCRECGRGFSRKSQLIIHQRTHTGEKPYVCGECGRGFIVESVLRNHLSTHSGEKPYVCSHCGRGFSCKPYLIRHQRTHTREKSFMCTVCGRGFREKSELIKHQRIHTGDKPYVCRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Phosphorylation	SLEQRNLYKEVMLEN CHHHHHHHHHHHHHH	14.51	24706070
157	Phosphorylation	GVRPLFWSTNERGAL CCCCCEEECCCCCCE	17.64	-
158	Phosphorylation	VRPLFWSTNERGALV CCCCEEECCCCCCEE	31.52	-
190	Phosphorylation	RILEIQLSPAQNASS EEEEEECCCCCCCCH	11.21	19664994
196	Phosphorylation	LSPAQNASSEEVDRI CCCCCCCCHHHHHHH	45.92	27251275
197	Phosphorylation	SPAQNASSEEVDRIS CCCCCCCHHHHHHHH	35.05	27251275
209	Phosphorylation	RISKRAETPGFGAVT HHHHCCCCCCCCCEE	27.94	-
260	Sumoylation	CGRGFSRKSQLIIHQ HCCCCCCCCEEEEEE	41.16	-
260	Sumoylation	CGRGFSRKSQLIIHQ HCCCCCCCCEEEEEE	41.16	-
269	Phosphorylation	QLIIHQRTHTGEKPY EEEEEECCCCCCCCE	19.74	-
271	Phosphorylation	IIHQRTHTGEKPYVC EEEECCCCCCCCEEC	46.56	-
274	Ubiquitination	QRTHTGEKPYVCGEC ECCCCCCCCEECCCC	42.89	-
274	Acetylation	QRTHTGEKPYVCGEC ECCCCCCCCEECCCC	42.89	7428825
276	Phosphorylation	THTGEKPYVCGECGR CCCCCCCEECCCCCC	21.31	-
299	Phosphorylation	RNHLSTHSGEKPYVC HHCCCCCCCCCCEEE	49.05	-
304	Phosphorylation	THSGEKPYVCSHCGR CCCCCCCEEECCCCC	25.75	-
355	Phosphorylation	IKHQRIHTGDKPYVC HHCCCCCCCCCCCCC	44.71	28555341
358	Acetylation	QRIHTGDKPYVCRD- CCCCCCCCCCCCCC-	39.32	30593823
358	Sumoylation	QRIHTGDKPYVCRD- CCCCCCCCCCCCCC-	39.32	-
358	Sumoylation	QRIHTGDKPYVCRD- CCCCCCCCCCCCCC-	39.32	-

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 ZN589_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN589_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 ZN589_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ZN589_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 ZN589_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY.	18691976 [Abstract]