dbPTM

ZC3H8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZC3H8_HUMAN
UniProt AC	Q8N5P1
Protein Name	Zinc finger CCCH domain-containing protein 8
Gene Name	ZC3H8
Organism	Homo sapiens (Human).
Sequence Length	291
Subcellular Localization	Nucleus . Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA gen
Protein Description	Acts as a transcriptional repressor of the GATA3 promoter. Sequence-specific DNA-binding factor that binds to the 5'-AGGTCTC-3' sequence within the negative cis-acting element intronic regulatory region (IRR) of the GATA3 gene (By similarity). Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III. [PubMed: 23932780 Induces thymocyte apoptosis when overexpressed, which may indicate a role in regulation of thymocyte homeostasis.]
Protein Sequence	MDFENLFSKPPNPALGKTATDSDERIDDEIDTEVEETQEEKIKLECEQIPKKFRHSAISPKSSLHRKSRSKDYDVYSDNDICSQESEDNFAKELQQYIQAREMANAAQPEESTKKEGVKDTPQAAKQKNKNLKAGHKNGKQKKMKRKWPGPGNKGSNALLRNSGSQEEDGKPKEKQQHLSQAFINQHTVERKGKQICKYFLERKCIKGDQCKFDHDAEIEKKKEMCKFYVQGYCTRGENCLYLHNEYPCKFYHTGTKCYQGEYCKFSHAPLTPETQELLAKVLDTEKKSCK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MDFENLFSKPPNPAL CCHHHHCCCCCCCCC	47.63	24719451
18	Phosphorylation	PNPALGKTATDSDER CCCCCCCCCCCCCHH	32.75	30278072
20	Phosphorylation	PALGKTATDSDERID CCCCCCCCCCCHHCC	41.07	30278072
22	Phosphorylation	LGKTATDSDERIDDE CCCCCCCCCHHCCHH	36.70	30278072
32	Phosphorylation	RIDDEIDTEVEETQE HCCHHHCCHHHHHHH	47.82	29255136
37	Phosphorylation	IDTEVEETQEEKIKL HCCHHHHHHHHHHHH	27.98	23403867
43	Sumoylation	ETQEEKIKLECEQIP HHHHHHHHHHHHHCC	49.67	-
43	Sumoylation	ETQEEKIKLECEQIP HHHHHHHHHHHHHCC	49.67	28112733
56	Phosphorylation	IPKKFRHSAISPKSS CCHHHCCCCCCCCHH	24.04	28176443
59	Phosphorylation	KFRHSAISPKSSLHR HHCCCCCCCCHHHCC	26.45	30266825
61	Ubiquitination	RHSAISPKSSLHRKS CCCCCCCCHHHCCCC	45.98	29967540
62	Phosphorylation	HSAISPKSSLHRKSR CCCCCCCHHHCCCCC	41.33	20068231
63	Phosphorylation	SAISPKSSLHRKSRS CCCCCCHHHCCCCCC	34.03	20068231
68	Phosphorylation	KSSLHRKSRSKDYDV CHHHCCCCCCCCCCC	41.57	-
70	Phosphorylation	SLHRKSRSKDYDVYS HHCCCCCCCCCCCCC	36.65	22167270
71	Methylation	LHRKSRSKDYDVYSD HCCCCCCCCCCCCCC	60.23	100332027
73	Phosphorylation	RKSRSKDYDVYSDND CCCCCCCCCCCCCCC	15.85	23927012
76	Phosphorylation	RSKDYDVYSDNDICS CCCCCCCCCCCCCCC	13.86	22167270
77	Phosphorylation	SKDYDVYSDNDICSQ CCCCCCCCCCCCCCC	29.77	22167270
83	Phosphorylation	YSDNDICSQESEDNF CCCCCCCCCCCHHHH	37.00	17525332
86	Phosphorylation	NDICSQESEDNFAKE CCCCCCCCHHHHHHH	42.48	23927012
97	Phosphorylation	FAKELQQYIQAREMA HHHHHHHHHHHHHHH	5.09	27642862
121	Phosphorylation	KKEGVKDTPQAAKQK HHCCCCCCHHHHHHH	16.16	30576142
140	Acetylation	KAGHKNGKQKKMKRK CHHCCCCCCCCCCCC	69.23	12637109
147	Acetylation	KQKKMKRKWPGPGNK CCCCCCCCCCCCCCH	52.82	7676549
163	Phosphorylation	SNALLRNSGSQEEDG HCHHHHCCCCCCCCC	33.13	30576142
165	Phosphorylation	ALLRNSGSQEEDGKP HHHHCCCCCCCCCCC	33.95	25849741
171	Acetylation	GSQEEDGKPKEKQQH CCCCCCCCCHHHHHH	66.30	26051181
175	Ubiquitination	EDGKPKEKQQHLSQA CCCCCHHHHHHHHHH	62.48	29967540
188	Phosphorylation	QAFINQHTVERKGKQ HHHHHHHHHHHHHHH	17.82	28555341
199	Phosphorylation	KGKQICKYFLERKCI HHHHHHHHHHHCCCC	14.69	20068231
229	Phosphorylation	KKEMCKFYVQGYCTR HHHHHHHHHCEEECC	4.20	-
254	Phosphorylation	YPCKFYHTGTKCYQG CCCEEEECCCCEECC	34.86	29396449
256	Phosphorylation	CKFYHTGTKCYQGEY CEEEECCCCEECCCC	21.06	29396449
272	Phosphorylation	KFSHAPLTPETQELL CCCCCCCCHHHHHHH	20.30	28348404

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
32	T	Phosphorylation	Kinase	CK2A1	P68400	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZC3H8_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 ZC3H8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LARP7_HUMAN	LARP7	physical	26186194
THUM1_HUMAN	THUMPD1	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
ZCRB1_HUMAN	ZCRB1	physical	26186194
CH033_HUMAN	C8orf33	physical	26186194
SF3B2_HUMAN	SF3B2	physical	26186194
THUM1_HUMAN	THUMPD1	physical	28514442
CH033_HUMAN	C8orf33	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
LARP7_HUMAN	LARP7	physical	28514442
RL7_HUMAN	RPL7	physical	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 ZC3H8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-77 AND SER-83, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, AND MASSSPECTROMETRY.	19690332 [Abstract]