ZN830_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN830_HUMAN
• UniProt AC: Q96NB3
• Protein Name: Zinc finger protein 830 {ECO:0000312|HGNC:HGNC:28291}
• Gene Name: ZNF830 {ECO:0000312|HGNC:HGNC:28291}
• Organism: Homo sapiens (Human).
• Sequence Length: 372
• Subcellular Localization: Nucleus . Chromosome . Nucleus speckle . Excluded from nucleolus.
• Protein Description: May play a role in pre-mRNA splicing as component of the spliceosome. [PubMed: 25599396 Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription (By similarity]
• Protein Sequence: MASSASARTPAGKRVINQEELRRLMKEKQRLSTSRKRIESPFAKYNRLGQLSCALCNTPVKSELLWQTHVLGKQHREKVAELKGAKEASQGSSASSAPHSVKRKAPDADDQDVKRAKATLVPQVQPSTSAWTTNFDKIGKEFIRATPSKPSGLSLLPDYEDEEEEEEEEEGDGERKRGDASKPLSDAQGKEHSVSSSREVTSSVLPNDFFSTNPPKAPIIPHSGSIEKAEIHEKVVERRENTAEALPEGFFDDPEVDARVRKVDAPKDQMDKEWDEFQKAMRQVNTISEAIVAEEDEEGRLDRQIGEIDEQIECYRRVEKLRNRQDEIKNKLKEILTIKELQKKEEENADSDDEGELQDLLSQDWRVKGALL

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
2	Acetylation	------MASSASART ------CCCCCCCCC	16.52	19413330
3	Phosphorylation	-----MASSASARTP -----CCCCCCCCCC	25.74	28122231
4	Phosphorylation	----MASSASARTPA ----CCCCCCCCCCC	19.39	28122231
6	Phosphorylation	--MASSASARTPAGK --CCCCCCCCCCCCC	21.89	29414761
9	Phosphorylation	ASSASARTPAGKRVI CCCCCCCCCCCCCCC	19.73	28450419
40	Phosphorylation	TSRKRIESPFAKYNR HHHHHCCCHHHHCCH	23.97	25159151
58	Phosphorylation	LSCALCNTPVKSELL HHHHCCCCCCCHHHH	28.58	21815630
89	Phosphorylation	LKGAKEASQGSSASS HHCHHHHHCCCCCCC	35.84	17525332
93	Phosphorylation	KEASQGSSASSAPHS HHHHCCCCCCCCCCC	38.71	-
100	Phosphorylation	SASSAPHSVKRKAPD CCCCCCCCCCCCCCC	28.42	25159151
114	Ubiquitination	DADDQDVKRAKATLV CCCHHHHHHHHHEEC	55.73	24816145
119	Phosphorylation	DVKRAKATLVPQVQP HHHHHHHEECCCCCC	27.81	-
129	O-linked_Glycosylation	PQVQPSTSAWTTNFD CCCCCCCCCCCCCHH	26.58	28510447
137	Acetylation	AWTTNFDKIGKEFIR CCCCCHHHHHHHHHH	49.58	26051181
146	Phosphorylation	GKEFIRATPSKPSGL HHHHHHCCCCCCCCC	20.46	25159151
148	Phosphorylation	EFIRATPSKPSGLSL HHHHCCCCCCCCCCC	53.49	18669648
149	Acetylation	FIRATPSKPSGLSLL HHHCCCCCCCCCCCC	44.39	26051181
159	Phosphorylation	GLSLLPDYEDEEEEE CCCCCCCCCCHHHHH	24.28	28796482
181	Phosphorylation	ERKRGDASKPLSDAQ CCCCCCCCCCCCHHC	39.28	24719451
190	Acetylation	PLSDAQGKEHSVSSS CCCHHCCCCCCCCCC	39.93	26051181
196	Phosphorylation	GKEHSVSSSREVTSS CCCCCCCCCCCCCCC	31.12	-
197	Phosphorylation	KEHSVSSSREVTSSV CCCCCCCCCCCCCCC	25.59	28985074
201	Phosphorylation	VSSSREVTSSVLPND CCCCCCCCCCCCCCC	15.55	28985074
223	Phosphorylation	KAPIIPHSGSIEKAE CCCCCCCCCCCCHHH	28.96	30266825
225	Phosphorylation	PIIPHSGSIEKAEIH CCCCCCCCCCHHHHH	30.50	30266825
234	Acetylation	EKAEIHEKVVERREN CHHHHHHHHHHHHHH	37.10	26051181
267	Acetylation	VRKVDAPKDQMDKEW HEECCCCHHHHHHHH	63.41	7926777
351	Phosphorylation	KEEENADSDDEGELQ HHHHCCCCCCHHHHH	44.55	22167270
362	Phosphorylation	GELQDLLSQDWRVKG HHHHHHHHCCCCHHC	33.13	17525332

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ZN830_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN830_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ZN830_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SF3B2_HUMAN	SF3B2	physical	22365833
ILF3_HUMAN	ILF3	physical	22365833
PRP8_HUMAN	PRPF8	physical	22365833
SNW1_HUMAN	SNW1	physical	22365833
AQR_HUMAN	AQR	physical	22365833
RED_HUMAN	IK	physical	22365833
PPIL2_HUMAN	PPIL2	physical	22365833
F10C1_HUMAN	FRA10AC1	physical	22365833
THOC5_HUMAN	THOC5	physical	22365833
PCBP1_HUMAN	PCBP1	physical	22365833
AQR_HUMAN	AQR	physical	26627737
SYF1_HUMAN	XAB2	physical	26627737
ISY1_HUMAN	ISY1	physical	26627737
PPIE_HUMAN	PPIE	physical	26627737
PPIL2_HUMAN	PPIL2	physical	26627737

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.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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 SER-351, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-351, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-89; SER-351 AND SER-362,AND MASS SPECTROMETRY.
PubMed: 17525332

"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-351, AND MASSSPECTROMETRY.
PubMed: 17081983