dbPTM

RAD17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAD17_HUMAN
UniProt AC	O75943
Protein Name	Cell cycle checkpoint protein RAD17
Gene Name	RAD17
Organism	Homo sapiens (Human).
Sequence Length	681
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..
Protein Sequence	MSKTFLRPKVSSTKVTDWVDPSFDDFLECSGVSTITATSLGVNNSSHRRKNGPSTLESSRFPARKRGNLSSLEQIYGLENSKEYLSENEPWVDKYKPETQHELAVHKKKIEEVETWLKAQVLERQPKQGGSILLITGPPGCGKTTTLKILSKEHGIQVQEWINPVLPDFQKDDFKGMFNTESSFHMFPYQSQIAVFKEFLLRATKYNKLQMLGDDLRTDKKIILVEDLPNQFYRDSHTLHEVLRKYVRIGRCPLIFIISDSLSGDNNQRLLFPKEIQEECSISNISFNPVAPTIMMKFLNRIVTIEANKNGGKITVPDKTSLELLCQGCSGDIRSAINSLQFSSSKGENNLRPRKKGMSLKSDAVLSKSKRRKKPDRVFENQEVQAIGGKDVSLFLFRALGKILYCKRASLTELDSPRLPSHLSEYERDTLLVEPEEVVEMSHMPGDLFNLYLHQNYIDFFMEIDDIVRASEFLSFADILSGDWNTRSLLREYSTSIATRGVMHSNKARGYAHCQGGGSSFRPLHKPQWFLINKKYRENCLAAKALFPDFCLPALCLQTQLLPYLALLTIPMRNQAQISFIQDIGRLPLKRHFGRLKMEALTDREHGMIDPDSGDEAQLNGGHSAEESLGEPTQATVPETWSLPLSQNSASELPASQPQPFSAQGDMEENIIIEDYESDGT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Ubiquitination	KVTDWVDPSFDDFLE CCCCCCCCCHHHHHH	27.55	29967540
32	Ubiquitination	DFLECSGVSTITATS HHHHHCCCCEEEEEE	2.34	29967540
45	Ubiquitination	TSLGVNNSSHRRKNG EEECCCCCCCCCCCC	23.47	29967540
54	Phosphorylation	HRRKNGPSTLESSRF CCCCCCCCCHHHCCC	47.20	28555341
55	Phosphorylation	RRKNGPSTLESSRFP CCCCCCCCHHHCCCC	37.36	17494752
55	Ubiquitination	RRKNGPSTLESSRFP CCCCCCCCHHHCCCC	37.36	29967540
59	Phosphorylation	GPSTLESSRFPARKR CCCCHHHCCCCCHHC	28.68	28555341
66	Methylation	SRFPARKRGNLSSLE CCCCCHHCCCCHHHH	33.41	115490083
70	Phosphorylation	ARKRGNLSSLEQIYG CHHCCCCHHHHHHHC	36.56	23898821
71	Phosphorylation	RKRGNLSSLEQIYGL HHCCCCHHHHHHHCC	38.81	23186163
71	Ubiquitination	RKRGNLSSLEQIYGL HHCCCCHHHHHHHCC	38.81	29967540
74	Ubiquitination	GNLSSLEQIYGLENS CCCHHHHHHHCCCCC	39.22	33845483
81	Phosphorylation	QIYGLENSKEYLSEN HHHCCCCCHHHHHCC	19.93	-
82	Ubiquitination	IYGLENSKEYLSENE HHCCCCCHHHHHCCC	63.06	29967540
83	Ubiquitination	YGLENSKEYLSENEP HCCCCCHHHHHCCCC	52.07	29967540
84	Phosphorylation	GLENSKEYLSENEPW CCCCCHHHHHCCCCC	21.18	23312004
85	Ubiquitination	LENSKEYLSENEPWV CCCCHHHHHCCCCCH	5.62	29967540
86	Phosphorylation	ENSKEYLSENEPWVD CCCHHHHHCCCCCHH	37.16	21815630
94	Ubiquitination	ENEPWVDKYKPETQH CCCCCHHHCCCCCHH	45.62	29967540
96	Ubiquitination	EPWVDKYKPETQHEL CCCHHHCCCCCHHCH	41.96	29967540
107	Ubiquitination	QHELAVHKKKIEEVE HHCHHHCHHHHHHHH	49.52	29967540
111	Ubiquitination	AVHKKKIEEVETWLK HHCHHHHHHHHHHHH	65.94	29967540
118	Ubiquitination	EEVETWLKAQVLERQ HHHHHHHHHHHHHHC	28.47	29967540
124	Ubiquitination	LKAQVLERQPKQGGS HHHHHHHHCCCCCCE	54.67	29967540
141	Ubiquitination	LITGPPGCGKTTTLK EEECCCCCCHHHHHH	6.61	29967540
143	Ubiquitination	TGPPGCGKTTTLKIL ECCCCCCHHHHHHHH	46.93	29967540
152	Ubiquitination	TTLKILSKEHGIQVQ HHHHHHHHHHCCCHH	50.73	29967540
160	Ubiquitination	EHGIQVQEWINPVLP HHCCCHHHHHCCCCC	52.01	33845483
170	Ubiquitination	NPVLPDFQKDDFKGM CCCCCCCCCCCCCCC	56.50	29967540
171	Ubiquitination	PVLPDFQKDDFKGMF CCCCCCCCCCCCCCC	60.29	33845483
197	Ubiquitination	QSQIAVFKEFLLRAT HHHHHHHHHHHHHHH	40.74	29967540
208	Ubiquitination	LRATKYNKLQMLGDD HHHHHHCCHHHCCCC	36.69	29967540
210	Ubiquitination	ATKYNKLQMLGDDLR HHHHCCHHHCCCCCC	27.02	29967540
221	Ubiquitination	DDLRTDKKIILVEDL CCCCCCCEEEEEECC	37.48	29967540
222	Ubiquitination	DLRTDKKIILVEDLP CCCCCCEEEEEECCC	3.47	29967540
249	Ubiquitination	VLRKYVRIGRCPLIF HHHHHHHHCCCCEEE	2.66	29967540
293	Phosphorylation	SFNPVAPTIMMKFLN CCCCCCHHHHHHHHH	16.27	17924679
304	Phosphorylation	KFLNRIVTIEANKNG HHHHHCEEEEECCCC	15.66	17924679
308	Ubiquitination	RIVTIEANKNGGKIT HCEEEEECCCCCEEE	26.07	29967540
319	Ubiquitination	GKITVPDKTSLELLC CEEECCCCCHHHHHH	33.66	29967540
335	Phosphorylation	GCSGDIRSAINSLQF CCCCCHHHHHHHHHC	33.56	-
335	Ubiquitination	GCSGDIRSAINSLQF CCCCCHHHHHHHHHC	33.56	29967540
346	Ubiquitination	SLQFSSSKGENNLRP HHHCCCCCCCCCCCC	72.67	29967540
359	Phosphorylation	RPRKKGMSLKSDAVL CCCCCCCCCCHHHHH	41.12	26074081
362	Phosphorylation	KKGMSLKSDAVLSKS CCCCCCCHHHHHCHH	35.77	-
367	Phosphorylation	LKSDAVLSKSKRRKK CCHHHHHCHHHCCCC	28.43	-
410	Phosphorylation	ILYCKRASLTELDSP HHHHCCCCCCCCCCC	39.60	29255136
412	Phosphorylation	YCKRASLTELDSPRL HHCCCCCCCCCCCCC	31.82	29255136
416	Phosphorylation	ASLTELDSPRLPSHL CCCCCCCCCCCCHHC	25.25	21815630
421	Ubiquitination	LDSPRLPSHLSEYER CCCCCCCHHCHHHCC	41.47	29967540
494	Phosphorylation	RSLLREYSTSIATRG HHHHHHHHHHHHHHC	15.78	28857561
500	Ubiquitination	YSTSIATRGVMHSNK HHHHHHHHCCCCCCC	27.04	29967540
579	Phosphorylation	MRNQAQISFIQDIGR CCCHHHHHHHHHHCC	12.29	26270265
586	Ubiquitination	SFIQDIGRLPLKRHF HHHHHHCCCCHHHHH	33.20	29967540
597	Ubiquitination	KRHFGRLKMEALTDR HHHHCHHHHHHHHCC	33.08	29967540
633	Phosphorylation	EESLGEPTQATVPET HHHCCCCCCCCCCCE	26.91	-
646	Phosphorylation	ETWSLPLSQNSASEL CEECCCCCCCCCCCC	25.94	14871926
656	Phosphorylation	SASELPASQPQPFSA CCCCCCCCCCCCCCC	40.22	11602352
676	Phosphorylation	ENIIIEDYESDGT-- CCEEEEECCCCCC--	12.44	-
678	Phosphorylation	IIIEDYESDGT---- EEEEECCCCCC----	34.80	-
681	Phosphorylation	EDYESDGT------- EECCCCCC-------	40.19	-

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
633	T	Phosphorylation	Kinase	ATM	Q13315	PSP
646	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
646	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
656	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
656	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
646	S	Phosphorylation	11418864
Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling.
656	S	Phosphorylation	11418864
Phosphorylation on Ser-646 and Ser-656 is cell cycle-regulated, enhanced by genotoxic stress, and required for activation of checkpoint signaling.

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 RAD17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFC2_HUMAN	RFC2	physical	14605214
RFC3_HUMAN	RFC3	physical	14605214
RFC4_HUMAN	RFC4	physical	14605214
RFC5_HUMAN	RFC5	physical	14605214
DPOE1_HUMAN	POLE	physical	14500819
DPOE2_HUMAN	POLE2	physical	14500819
DPOE3_HUMAN	POLE3	physical	14500819
DPOE4_HUMAN	POLE4	physical	14500819
RAD9A_HUMAN	RAD9A	physical	12578958
HUS1_HUMAN	HUS1	physical	12578958
RAD1_HUMAN	RAD1	physical	12578958
RAD9A_HUMAN	RAD9A	physical	10884395
HUS1_HUMAN	HUS1	physical	10884395
RAD1_HUMAN	RAD1	physical	10884395
NH2L1_HUMAN	NHP2L1	physical	10593953
RAD1_HUMAN	RAD1	physical	11418864
CLSPN_HUMAN	CLSPN	physical	16885023
CADH1_HUMAN	CDH1	physical	20424596
ANM6_HUMAN	PRMT6	physical	23455924
UBP20_HUMAN	USP20	physical	24923443
RFC4_HUMAN	RFC4	physical	28514442
RFC3_HUMAN	RFC3	physical	28514442
RFC2_HUMAN	RFC2	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 RAD17_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, MUTAGENESIS OFSER-646 AND SER-656, AND INTERACTION WITH POLE.	14500819 [Abstract]
"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: FUNCTION, PHOSPHORYLATION AT SER-646 AND SER-656, INTERACTION WITHRFC4, AND MUTAGENESIS OF SER-191; SER-646 AND SER-656.	11687627 [Abstract]
"ATR/ATM-mediated phosphorylation of human Rad17 is required forgenotoxic stress responses."; Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A.,Ali A., Chen S.M., Abraham R.T., Wang X.-F.; Nature 411:969-974(2001). Cited for: FUNCTION, INTERACTION WITH ATM; ATR AND RAD1, PHOSPHORYLATION ATSER-646 AND SER-656, AND MUTAGENESIS OF SER-646 AND SER-656.	11418864 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, AND MASSSPECTROMETRY.	17924679 [Abstract]

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