dbPTM

ZN239_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN239_HUMAN
UniProt AC	Q16600
Protein Name	Zinc finger protein 239
Gene Name	ZNF239
Organism	Homo sapiens (Human).
Sequence Length	458
Subcellular Localization	Nucleus .
Protein Description	May be involved in transcriptional regulation..
Protein Sequence	MASTITGSQDCIVNHRGEVDGEPELDISPCQQWGEASSPISRNRDSVMTLQSGCFENIESETYLPLKVSSQIDTQDSSVKFCKNEPQDHQESRRLFVMEESTERKVIKGESCSENLQVKLVSDGQELASPLLNGEATCQNGQLKESLDPIDCNCKDIHGWKSQVVSCSQQRAHTEEKPCDHNNCGKILNTSPDGHPYEKIHTAEKQYECSQCGKNFSQSSELLLHQRDHTEEKPYKCEQCGKGFTRSSSLLIHQAVHTDEKPYKCDKCGKGFTRSSSLLIHHAVHTGEKPYKCDKCGKGFSQSSKLHIHQRVHTGEKPYECEECGMSFSQRSNLHIHQRVHTGERPYKCGECGKGFSQSSNLHIHRCIHTGEKPYQCYECGKGFSQSSDLRIHLRVHTGEKPYHCGKCGKGFSQSSKLLIHQRVHTGEKPYECSKCGKGFSQSSNLHIHQRVHKKDPR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MASTITGSQDCIV --CCCCCCCCCCEEE	30.76	28348404
8	Phosphorylation	MASTITGSQDCIVNH CCCCCCCCCCEEECC	17.75	28348404
28	Phosphorylation	GEPELDISPCQQWGE CCCCCCCCCCCCCCC	21.20	25159151
37	Phosphorylation	CQQWGEASSPISRNR CCCCCCCCCCCCCCH	32.14	28348404
38	Phosphorylation	QQWGEASSPISRNRD CCCCCCCCCCCCCHH	33.04	25159151
41	Phosphorylation	GEASSPISRNRDSVM CCCCCCCCCCHHHCE	27.21	27251275
74	Phosphorylation	KVSSQIDTQDSSVKF EEECCCCCCCCCCEE	35.59	30576142
108	Sumoylation	STERKVIKGESCSEN CCCCEEECCCCCCCC	60.66	-
108	Sumoylation	STERKVIKGESCSEN CCCCEEECCCCCCCC	60.66	28112733
168	Phosphorylation	KSQVVSCSQQRAHTE HHHEEEHHHHCCCCC	23.11	-
190	Phosphorylation	NCGKILNTSPDGHPY CCCCCCCCCCCCCCC	37.89	30266825
191	Phosphorylation	CGKILNTSPDGHPYE CCCCCCCCCCCCCCH	21.66	30266825
197	Phosphorylation	TSPDGHPYEKIHTAE CCCCCCCCHHCCCHH	24.95	30266825
236	Sumoylation	HTEEKPYKCEQCGKG CCCCCCCCCCCCCCC	39.56	-
236	Sumoylation	HTEEKPYKCEQCGKG CCCCCCCCCCCCCCC	39.56	-
247	Phosphorylation	CGKGFTRSSSLLIHQ CCCCCCCCHHHHEEE	22.63	21712546
248	Phosphorylation	GKGFTRSSSLLIHQA CCCCCCCHHHHEEEE	23.01	29523821
249	Phosphorylation	KGFTRSSSLLIHQAV CCCCCCHHHHEEEEE	28.57	29523821
258	Phosphorylation	LIHQAVHTDEKPYKC HEEEEEECCCCCCCC	38.97	26055452
275	Phosphorylation	CGKGFTRSSSLLIHH CCCCCCCCHHHHEEE	22.63	28348404
276	Phosphorylation	GKGFTRSSSLLIHHA CCCCCCCHHHHEEEH	23.01	24719451
277	Phosphorylation	KGFTRSSSLLIHHAV CCCCCCHHHHEEEHH	28.57	26425664
286	Phosphorylation	LIHHAVHTGEKPYKC HEEEHHHCCCCCCCC	40.20	29496963
289	Sumoylation	HAVHTGEKPYKCDKC EHHHCCCCCCCCCCC	55.80	-
289	Sumoylation	HAVHTGEKPYKCDKC EHHHCCCCCCCCCCC	55.80	-
289	Ubiquitination	HAVHTGEKPYKCDKC EHHHCCCCCCCCCCC	55.80	-
291	Phosphorylation	VHTGEKPYKCDKCGK HHCCCCCCCCCCCCC	35.00	-
301	Phosphorylation	DKCGKGFSQSSKLHI CCCCCCCCCCCCEEE	37.51	22210691
303	Phosphorylation	CGKGFSQSSKLHIHQ CCCCCCCCCCEEEEE	28.39	22210691
314	Phosphorylation	HIHQRVHTGEKPYEC EEEEECCCCCCCEEC	44.15	29214152
342	Phosphorylation	HIHQRVHTGERPYKC EECCCCCCCCCCEEC	37.57	27251275
348	Sumoylation	HTGERPYKCGECGKG CCCCCCEECCCCCCC	38.15	-
348	Sumoylation	HTGERPYKCGECGKG CCCCCCEECCCCCCC	38.15	-
357	Phosphorylation	GECGKGFSQSSNLHI CCCCCCCCCCCCEEE	37.51	28555341
359	Phosphorylation	CGKGFSQSSNLHIHR CCCCCCCCCCEEEEE	21.72	28555341
370	Phosphorylation	HIHRCIHTGEKPYQC EEEEEEECCCCCEEE	27.42	-
398	Phosphorylation	RIHLRVHTGEKPYHC EEEEEEECCCCCCCC	44.15	-
413	Phosphorylation	GKCGKGFSQSSKLLI CCCCCCCCCCCCEEE	37.51	22210691
415	Phosphorylation	CGKGFSQSSKLLIHQ CCCCCCCCCCEEEEE	28.39	22210691
426	Phosphorylation	LIHQRVHTGEKPYEC EEEEEECCCCCCCCC	44.15	29496963

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
38	S	Phosphorylation	Kinase	MAPK10	P53779	GPS
46	S	Phosphorylation	Kinase	AURKA	O14965	GPS
46	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
129	S	Phosphorylation	Kinase	MAPK10	P53779	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN239_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 ZN239_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CEP70_HUMAN	CEP70	physical	25416956

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 ZN239_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-41, AND MASSSPECTROMETRY.	17081983 [Abstract]