RAD17_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAD17_MOUSE
• UniProt AC: Q6NXW6
• Protein Name: Cell cycle checkpoint protein RAD17
• Gene Name: Rad17
• Organism: Mus musculus (Mouse).
• Sequence Length: 688
• Subcellular Localization: Nucleus. Phosphorylated form redistributes to discrete nuclear foci upon DNA damage..
• Protein Description: Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9-HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination (By similarity). Essential for embryonic development. May be involved in homologous recombination..
• Protein Sequence: MSETFLRPKVSSTKVTDWVAPAFDDFEANTAITTITASSLTFSNSSHRRKYLPSTLESNRLSARKRGRLSLEQTHGLETSRERLSDNEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLEVKPKQGGSVLLITGPPGCGKTTTIKILSKELGIQVQEWVNPILPDFQKDDYKELLSLESNFSVVPYQSQIAVFNDFLLRATKYSKLQMLGDDLTTDKKIILVEELPNQFYRDPNALHEILRKHVQIGRCPLVFIVSDSVSGDNNQRLLFPRNIQEECSVSNISFNPVAPTIMMKFLNRIVTIEASKNGEKIIVPNKTSLELLCQGCSGDIRSAINSLQFSSSKGENSSWSKKKRMSLKSDAAISKSKQKKKHNSTLENQEIQAIGGKDVSLFLFRALGKILYCKRAPLTELDSPRLPAHLSEHDRDTLLVQPEEIVEMSHMPGDFFNLYLHQNYIDFFAEVDDLVPASEFLSFADILGGDWNTRSLLREYSTSVATRGVMHSNKARGFAHCQGGSSFRPLHKPQWFLIQKKYRENCLAAKALFVDFCLPALCLQTQLLPYLALLTIPMRNKAQISFIQDVGRLPLKRSFGRLKMEALTDRELGLIDPDSGDESPHSGGQPAQEAPGEPAQAAQNADPETWSLPLSQNSGSDLPASQPQPFSSKVDMEEEEEEEEDIIIEDYDSEET

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
55	Phosphorylation	RRKYLPSTLESNRLS HHHCCCCHHHHCCCC	32.38	-
70	Phosphorylation	ARKRGRLSLEQTHGL HHHHCCCCHHHHCCC	28.62	24704852
74	Phosphorylation	GRLSLEQTHGLETSR CCCCHHHHCCCCHHH	14.45	28066266
85	Phosphorylation	ETSRERLSDNEPWVD CHHHHHHCCCCCCHH	44.61	28066266
93	Acetylation	DNEPWVDKYKPETQH CCCCCHHHCCCCCHH	45.62	23236377
358	Phosphorylation	WSKKKRMSLKSDAAI CCHHHHHCHHHHHHH	36.36	-
411	Phosphorylation	YCKRAPLTELDSPRL HEECCCCCCCCCCCC	33.18	28066266
415	Phosphorylation	APLTELDSPRLPAHL CCCCCCCCCCCCCCC	25.25	28066266
498	Phosphorylation	EYSTSVATRGVMHSN HHCCCCHHHCCCCCC	26.29	22871156
504	Phosphorylation	ATRGVMHSNKARGFA HHHCCCCCCCCCCCE	23.17	22871156
647	Phosphorylation	ETWSLPLSQNSGSDL CCCCCCCCCCCCCCC	25.94	14500819
657	Phosphorylation	SGSDLPASQPQPFSS CCCCCCCCCCCCCCC	40.22	14500819

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
647	S	Phosphorylation	Kinase	ATR	Q9JKK8	Uniprot
657	S	Phosphorylation	Kinase	ATR	Q9JKK8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
647	S	Phosphorylation	Phosphorylation on Ser-647 and Ser-657 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling.	11687627
657	S	Phosphorylation	Phosphorylation on Ser-647 and Ser-657 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling.	11687627

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAD17_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PK3CB_MOUSE	Pik3cb	physical	20368419

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The human checkpoint Rad protein Rad17 is chromatin-associatedthroughout the cell cycle, localizes to DNA replication sites, andinteracts with DNA polymerase epsilon.";
Post S.M., Tomkinson A.E., Lee E.Y.-H.P.;
Nucleic Acids Res. 31:5568-5575(2003).
Cited for: PHOSPHORYLATION AT SER-647 AND SER-657.
PubMed: 14500819

"Phosphorylation of serines 635 and 645 of human Rad17 is cell cycleregulated and is required for G(1)/S checkpoint activation in responseto DNA damage.";
Post S.M., Weng Y.-C., Cimprich K., Chen L.B., Xu Y., Lee E.Y.-H.P.;
Proc. Natl. Acad. Sci. U.S.A. 98:13102-13107(2001).
Cited for: PHOSPHORYLATION AT SER-647 AND SER-657.
PubMed: 11687627