dbPTM

RAD18_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAD18_HUMAN
UniProt AC	Q9NS91
Protein Name	E3 ubiquitin-protein ligase RAD18
Gene Name	RAD18
Organism	Homo sapiens (Human).
Sequence Length	495
Subcellular Localization	Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Associates with chromatin (PubMed:25931565). Colocalizes with SLF1 in the nucleus and to centrosomes (PubMed:15632077). Relocalizes with SLF1 to nuclear foci in response t
Protein Description	E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity..
Protein Sequence	MDSLAESRWPPGLAVMKTIDDLLRCGICFEYFNIAMIIPQCSHNYCSLCIRKFLSYKTQCPTCCVTVTEPDLKNNRILDELVKSLNFARNHLLQFALESPAKSPASSSSKNLAVKVYTPVASRQSLKQGSRLMDNFLIREMSGSTSELLIKENKSKFSPQKEASPAAKTKETRSVEEIAPDPSEAKRPEPPSTSTLKQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKRKPLPKTVYNLLSDRDLKKKLKEHGLSIQGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEIVREIENIEKTRMRLEASKLNESVMVFTKDQTEKEIDEIHSKYRKKHKSEFQLLVDQARKGYKKIAGMSQKTVTITKEDESTEKLSSVCMGQEDNMTSVTNHFSQSKLDSPEELEPDREEDSSSCIDIQEVLSSSESDSCNSSSSDIIRDLLEEEEAWEASHKNDLQDTEISPRQNRRTRAAESAEIEPRNKRNRN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSLAESR -------CCCHHHHC	7.73	22814378
16	Ubiquitination	WPPGLAVMKTIDDLL CCCCHHHHHHHHHHH	2.36	21890473
17	Ubiquitination	PPGLAVMKTIDDLLR CCCHHHHHHHHHHHH	35.41	33845483
24	Ubiquitination	KTIDDLLRCGICFEY HHHHHHHHCCCCHHH	24.74	23000965
29	Ubiquitination	LLRCGICFEYFNIAM HHHCCCCHHHCCEEE	8.90	23000965
41	Ubiquitination	IAMIIPQCSHNYCSL EEEECHHCCCCCHHH	3.61	27667366
52	Acetylation	YCSLCIRKFLSYKTQ CHHHHHHHHHHCCCC	30.64	26051181
52	Ubiquitination	YCSLCIRKFLSYKTQ CHHHHHHHHHHCCCC	30.64	21963094
55	Phosphorylation	LCIRKFLSYKTQCPT HHHHHHHHCCCCCCC	27.93	28152594
56	Phosphorylation	CIRKFLSYKTQCPTC HHHHHHHCCCCCCCE	21.87	25884760
57	Acetylation	IRKFLSYKTQCPTCC HHHHHHCCCCCCCEE	28.83	26051181
57	Ubiquitination	IRKFLSYKTQCPTCC HHHHHHCCCCCCCEE	28.83	21963094
58	Phosphorylation	RKFLSYKTQCPTCCV HHHHHCCCCCCCEEE	27.46	28152594
62	Phosphorylation	SYKTQCPTCCVTVTE HCCCCCCCEEEEECC	26.60	28152594
65	Ubiquitination	TQCPTCCVTVTEPDL CCCCCEEEEECCCCC	5.40	23000965
66	Phosphorylation	QCPTCCVTVTEPDLK CCCCEEEEECCCCCC	14.06	28152594
68	Ubiquitination	PTCCVTVTEPDLKNN CCEEEEECCCCCCCC	32.22	23000965
70	Ubiquitination	CCVTVTEPDLKNNRI EEEEECCCCCCCCHH	42.75	23000965
73	Ubiquitination	TVTEPDLKNNRILDE EECCCCCCCCHHHHH	60.60	21963094
75	Ubiquitination	TEPDLKNNRILDELV CCCCCCCCHHHHHHH	30.68	23000965
82	Ubiquitination	NRILDELVKSLNFAR CHHHHHHHHHHHHHH	3.58	22817900
83	Ubiquitination	RILDELVKSLNFARN HHHHHHHHHHHHHHH	62.95	23000965
84	Ubiquitination	ILDELVKSLNFARNH HHHHHHHHHHHHHHH	22.52	22817900
99	Phosphorylation	LLQFALESPAKSPAS HHHHHHHCCCCCCCC	30.89	22167270
100	Ubiquitination	LQFALESPAKSPASS HHHHHHCCCCCCCCC	34.04	23000965
102	Sumoylation	FALESPAKSPASSSS HHHHCCCCCCCCCCC	61.43	-
102	Sumoylation	FALESPAKSPASSSS HHHHCCCCCCCCCCC	61.43	-
102	Ubiquitination	FALESPAKSPASSSS HHHHCCCCCCCCCCC	61.43	21963094
103	Phosphorylation	ALESPAKSPASSSSK HHHCCCCCCCCCCCC	28.01	23927012
106	Phosphorylation	SPAKSPASSSSKNLA CCCCCCCCCCCCCEE	33.85	26503892
107	Phosphorylation	PAKSPASSSSKNLAV CCCCCCCCCCCCEEE	40.51	23927012
108	Phosphorylation	AKSPASSSSKNLAVK CCCCCCCCCCCEEEE	42.72	23927012
109	Phosphorylation	KSPASSSSKNLAVKV CCCCCCCCCCEEEEE	27.75	23927012
110	Sumoylation	SPASSSSKNLAVKVY CCCCCCCCCEEEEEE	58.91	-
110	Sumoylation	SPASSSSKNLAVKVY CCCCCCCCCEEEEEE	58.91	-
110	Ubiquitination	SPASSSSKNLAVKVY CCCCCCCCCEEEEEE	58.91	23000965
111	Ubiquitination	PASSSSKNLAVKVYT CCCCCCCCEEEEEEC	34.87	23000965
115	Sumoylation	SSKNLAVKVYTPVAS CCCCEEEEEECCCCC	24.74	-
115	Sumoylation	SSKNLAVKVYTPVAS CCCCEEEEEECCCCC	24.74	-
115	Ubiquitination	SSKNLAVKVYTPVAS CCCCEEEEEECCCCC	24.74	23000965
117	Phosphorylation	KNLAVKVYTPVASRQ CCEEEEEECCCCCHH	10.29	28796482
118	Phosphorylation	NLAVKVYTPVASRQS CEEEEEECCCCCHHH	17.80	25159151
122	Phosphorylation	KVYTPVASRQSLKQG EEECCCCCHHHHHHC	30.96	25159151
125	Phosphorylation	TPVASRQSLKQGSRL CCCCCHHHHHHCCCH	36.10	25159151
127	Sumoylation	VASRQSLKQGSRLMD CCCHHHHHHCCCHHH	58.84	-
127	Sumoylation	VASRQSLKQGSRLMD CCCHHHHHHCCCHHH	58.84	-
127	Ubiquitination	VASRQSLKQGSRLMD CCCHHHHHHCCCHHH	58.84	27667366
130	O-linked_Glycosylation	RQSLKQGSRLMDNFL HHHHHHCCCHHHHHH	21.53	30379171
132	Ubiquitination	SLKQGSRLMDNFLIR HHHHCCCHHHHHHHH	5.60	21963094
141	Sulfoxidation	DNFLIREMSGSTSEL HHHHHHHCCCCHHHH	3.85	21406390
142	Phosphorylation	NFLIREMSGSTSELL HHHHHHCCCCHHHHH	25.49	25159151
144	Phosphorylation	LIREMSGSTSELLIK HHHHCCCCHHHHHHH	22.81	28555341
145	Phosphorylation	IREMSGSTSELLIKE HHHCCCCHHHHHHHH	29.73	26074081
146	Phosphorylation	REMSGSTSELLIKEN HHCCCCHHHHHHHHC	28.13	26074081
151	Sumoylation	STSELLIKENKSKFS CHHHHHHHHCHHCCC	56.03	-
151	Sumoylation	STSELLIKENKSKFS CHHHHHHHHCHHCCC	56.03	-
151	Ubiquitination	STSELLIKENKSKFS CHHHHHHHHCHHCCC	56.03	23000965
153	Ubiquitination	SELLIKENKSKFSPQ HHHHHHHCHHCCCCC	49.23	23000965
154	Ubiquitination	ELLIKENKSKFSPQK HHHHHHCHHCCCCCC	56.99	23000965
155	Phosphorylation	LLIKENKSKFSPQKE HHHHHCHHCCCCCCC	50.98	30266825
155	Ubiquitination	LLIKENKSKFSPQKE HHHHHCHHCCCCCCC	50.98	23000965
156	Ubiquitination	LIKENKSKFSPQKEA HHHHCHHCCCCCCCC	52.01	23000965
158	Phosphorylation	KENKSKFSPQKEASP HHCHHCCCCCCCCCC	30.11	23401153
159	Ubiquitination	ENKSKFSPQKEASPA HCHHCCCCCCCCCCC	53.01	21890473
161	Ubiquitination	KSKFSPQKEASPAAK HHCCCCCCCCCCCCC	59.64	23000965
164	O-linked_Glycosylation	FSPQKEASPAAKTKE CCCCCCCCCCCCCCC	19.03	30379171
164	Phosphorylation	FSPQKEASPAAKTKE CCCCCCCCCCCCCCC	19.03	23401153
168	Ubiquitination	KEASPAAKTKETRSV CCCCCCCCCCCCCCH	63.34	21906983
169	Phosphorylation	EASPAAKTKETRSVE CCCCCCCCCCCCCHH	29.41	29449344
170	Ubiquitination	ASPAAKTKETRSVEE CCCCCCCCCCCCHHH	57.28	22817900
171	Ubiquitination	SPAAKTKETRSVEEI CCCCCCCCCCCHHHH	55.47	22817900
172	Phosphorylation	PAAKTKETRSVEEIA CCCCCCCCCCHHHHC	29.78	25627689
172	Ubiquitination	PAAKTKETRSVEEIA CCCCCCCCCCHHHHC	29.78	22817900
173	Ubiquitination	AAKTKETRSVEEIAP CCCCCCCCCHHHHCC	39.53	22817900
174	Phosphorylation	AKTKETRSVEEIAPD CCCCCCCCHHHHCCC	41.10	20873877
175	Ubiquitination	KTKETRSVEEIAPDP CCCCCCCHHHHCCCH	7.44	21963094
185	Ubiquitination	IAPDPSEAKRPEPPS HCCCHHHCCCCCCCC	19.93	21890473
186	Sumoylation	APDPSEAKRPEPPST CCCHHHCCCCCCCCC	65.52	-
186	Sumoylation	APDPSEAKRPEPPST CCCHHHCCCCCCCCC	65.52	-
186	Ubiquitination	APDPSEAKRPEPPST CCCHHHCCCCCCCCC	65.52	23000965
190	Ubiquitination	SEAKRPEPPSTSTLK HHCCCCCCCCCCCCC	30.72	22817900
192	Phosphorylation	AKRPEPPSTSTLKQV CCCCCCCCCCCCCCC	45.78	28555341
194	Phosphorylation	RPEPPSTSTLKQVTK CCCCCCCCCCCCCCC	35.76	25627689
195	Phosphorylation	PEPPSTSTLKQVTKV CCCCCCCCCCCCCCC	37.75	25627689
197	Sumoylation	PPSTSTLKQVTKVDC CCCCCCCCCCCCCCC	42.69	-
197	Sumoylation	PPSTSTLKQVTKVDC CCCCCCCCCCCCCCC	42.69	-
197	Ubiquitination	PPSTSTLKQVTKVDC CCCCCCCCCCCCCCC	42.69	23000965
201	Sumoylation	STLKQVTKVDCPVCG CCCCCCCCCCCCCCC	36.90	-
201	Sumoylation	STLKQVTKVDCPVCG CCCCCCCCCCCCCCC	36.90	-
201	Ubiquitination	STLKQVTKVDCPVCG CCCCCCCCCCCCCCC	36.90	23000965
218	Ubiquitination	IPESHINKHLDSCLS CCHHHHHHHHHHHCC	44.96	21906983
223	Ubiquitination	INKHLDSCLSREEKK HHHHHHHHCCHHHHH	3.90	23000965
229	Sumoylation	SCLSREEKKESLRSS HHCCHHHHHHHHHHH	58.02	-
229	Sumoylation	SCLSREEKKESLRSS HHCCHHHHHHHHHHH	58.02	-
229	Ubiquitination	SCLSREEKKESLRSS HHCCHHHHHHHHHHH	58.02	-
232	Ubiquitination	SREEKKESLRSSVHK CHHHHHHHHHHHHHC	37.65	23000965
235	Phosphorylation	EKKESLRSSVHKRKP HHHHHHHHHHHCCCC	41.84	25627689
236	Phosphorylation	KKESLRSSVHKRKPL HHHHHHHHHHCCCCC	23.08	28348404
239	Ubiquitination	SLRSSVHKRKPLPKT HHHHHHHCCCCCCHH	61.02	23000965
241	Acetylation	RSSVHKRKPLPKTVY HHHHHCCCCCCHHHH	56.56	26051181
241	Ubiquitination	RSSVHKRKPLPKTVY HHHHHCCCCCCHHHH	56.56	23000965
242	Ubiquitination	SSVHKRKPLPKTVYN HHHHCCCCCCHHHHH	58.91	23000965
245	Ubiquitination	HKRKPLPKTVYNLLS HCCCCCCHHHHHHCC	59.30	23000965
247	Ubiquitination	RKPLPKTVYNLLSDR CCCCCHHHHHHCCCH	3.58	23000965
254	Methylation	VYNLLSDRDLKKKLK HHHHCCCHHHHHHHH	48.03	115490091
255	Ubiquitination	YNLLSDRDLKKKLKE HHHCCCHHHHHHHHH	68.76	23000965
257	Sumoylation	LLSDRDLKKKLKEHG HCCCHHHHHHHHHCC	52.75	-
257	Sumoylation	LLSDRDLKKKLKEHG HCCCHHHHHHHHHCC	52.75	-
257	Ubiquitination	LLSDRDLKKKLKEHG HCCCHHHHHHHHHCC	52.75	21906983
258	Ubiquitination	LSDRDLKKKLKEHGL CCCHHHHHHHHHCCC	71.31	23000965
259	Ubiquitination	SDRDLKKKLKEHGLS CCHHHHHHHHHCCCC	64.30	23000965
261	Sumoylation	RDLKKKLKEHGLSIQ HHHHHHHHHCCCCCC	57.45	-
261	Sumoylation	RDLKKKLKEHGLSIQ HHHHHHHHHCCCCCC	57.45	-
261	Ubiquitination	RDLKKKLKEHGLSIQ HHHHHHHHHCCCCCC	57.45	23000965
271	Ubiquitination	GLSIQGNKQQLIKRH CCCCCCCHHHHHHHH	46.36	27667366
276	Ubiquitination	GNKQQLIKRHQEFVH CCHHHHHHHHHHHHH	53.04	22817900
284	Ubiquitination	RHQEFVHMYNAQCDA HHHHHHHHHHHCCCC	2.01	21890473
290	Ubiquitination	HMYNAQCDALHPKSA HHHHHCCCCCCCCCH	39.83	21963094
297	Ubiquitination	DALHPKSAAEIVREI CCCCCCCHHHHHHHH	18.42	21963094
309	Ubiquitination	REIENIEKTRMRLEA HHHHHHHHHHHHHHH	37.32	23000965
318	Sumoylation	RMRLEASKLNESVMV HHHHHHHHCCCCEEE	63.48	-
318	Sumoylation	RMRLEASKLNESVMV HHHHHHHHCCCCEEE	63.48	-
318	Ubiquitination	RMRLEASKLNESVMV HHHHHHHHCCCCEEE	63.48	23000965
322	Phosphorylation	EASKLNESVMVFTKD HHHHCCCCEEEEECC	17.91	30266825
327	Phosphorylation	NESVMVFTKDQTEKE CCCEEEEECCCCHHH	23.46	30266825
328	Sumoylation	ESVMVFTKDQTEKEI CCEEEEECCCCHHHH	36.05	-
328	Sumoylation	ESVMVFTKDQTEKEI CCEEEEECCCCHHHH	36.05	-
328	Ubiquitination	ESVMVFTKDQTEKEI CCEEEEECCCCHHHH	36.05	23000965
333	Ubiquitination	FTKDQTEKEIDEIHS EECCCCHHHHHHHHH	64.46	23000965
341	Acetylation	EIDEIHSKYRKKHKS HHHHHHHHHHHHCHH	34.61	26051181
341	Ubiquitination	EIDEIHSKYRKKHKS HHHHHHHHHHHHCHH	34.61	23000965
344	Ubiquitination	EIHSKYRKKHKSEFQ HHHHHHHHHCHHHHH	57.02	23000965
345	Ubiquitination	IHSKYRKKHKSEFQL HHHHHHHHCHHHHHH	47.47	23000965
347	Sumoylation	SKYRKKHKSEFQLLV HHHHHHCHHHHHHHH	61.64	-
347	Sumoylation	SKYRKKHKSEFQLLV HHHHHHCHHHHHHHH	61.64	-
347	Ubiquitination	SKYRKKHKSEFQLLV HHHHHHCHHHHHHHH	61.64	23000965
348	Phosphorylation	KYRKKHKSEFQLLVD HHHHHCHHHHHHHHH	43.28	28555341
362	Ubiquitination	DQARKGYKKIAGMSQ HHHHHHHHHHHCCCC	46.50	-
363	Ubiquitination	QARKGYKKIAGMSQK HHHHHHHHHHCCCCC	29.34	29967540
368	Phosphorylation	YKKIAGMSQKTVTIT HHHHHCCCCCEEEEE	27.83	23403867
370	Sumoylation	KIAGMSQKTVTITKE HHHCCCCCEEEEECC	37.34	-
370	Acetylation	KIAGMSQKTVTITKE HHHCCCCCEEEEECC	37.34	71255
370	Sumoylation	KIAGMSQKTVTITKE HHHCCCCCEEEEECC	37.34	-
370	Ubiquitination	KIAGMSQKTVTITKE HHHCCCCCEEEEECC	37.34	22817900
375	Phosphorylation	SQKTVTITKEDESTE CCCEEEEECCCCCCH	21.00	23403867
376	Sumoylation	QKTVTITKEDESTEK CCEEEEECCCCCCHH	60.36	-
376	Acetylation	QKTVTITKEDESTEK CCEEEEECCCCCCHH	60.36	26051181
376	Sumoylation	QKTVTITKEDESTEK CCEEEEECCCCCCHH	60.36	28112733
376	Ubiquitination	QKTVTITKEDESTEK CCEEEEECCCCCCHH	60.36	21906983
380	Phosphorylation	TITKEDESTEKLSSV EEECCCCCCHHHHHH	54.94	20860994
383	Ubiquitination	KEDESTEKLSSVCMG CCCCCCHHHHHHHCC	54.48	21963094
385	Phosphorylation	DESTEKLSSVCMGQE CCCCHHHHHHHCCCC	31.62	20068231
386	Phosphorylation	ESTEKLSSVCMGQED CCCHHHHHHHCCCCC	29.76	30576142
396	Phosphorylation	MGQEDNMTSVTNHFS CCCCCCCHHHHHCCC	26.71	20068231
397	Phosphorylation	GQEDNMTSVTNHFSQ CCCCCCHHHHHCCCH	19.04	30576142
399	Phosphorylation	EDNMTSVTNHFSQSK CCCCHHHHHCCCHHH	23.81	30576142
403	Phosphorylation	TSVTNHFSQSKLDSP HHHHHCCCHHHCCCH	26.45	17525332
405	Phosphorylation	VTNHFSQSKLDSPEE HHHCCCHHHCCCHHH	33.71	25159151
409	Phosphorylation	FSQSKLDSPEELEPD CCHHHCCCHHHCCCC	44.65	29255136
434	Phosphorylation	IQEVLSSSESDSCNS HHHHHHCCCCCCCCC	37.43	21098111
460	Phosphorylation	EEEAWEASHKNDLQD HHHHHHHHHHCCCCC	24.39	26074081
462	Ubiquitination	EAWEASHKNDLQDTE HHHHHHHHCCCCCCC	50.06	21906983
468	O-linked_Glycosylation	HKNDLQDTEISPRQN HHCCCCCCCCCHHHC	23.43	30379171
468	Phosphorylation	HKNDLQDTEISPRQN HHCCCCCCCCCHHHC	23.43	23927012
471	Phosphorylation	DLQDTEISPRQNRRT CCCCCCCCHHHCHHH	14.06	19664994
478	Phosphorylation	SPRQNRRTRAAESAE CHHHCHHHHHHHHHC	22.79	26074081
483	Phosphorylation	RRTRAAESAEIEPRN HHHHHHHHHCCCCCC	26.86	25218447

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
99	S	Phosphorylation	Kinase	CDK2	P24941	PSP
403	S	Phosphorylation	Kinase	ATM	Q13315	PSP
434	S	Phosphorylation	Kinase	CDC7	O00311	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RAD18	Q9NS91	PMID:15509568

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAD18_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 RAD18_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE2A_HUMAN	UBE2A	physical	10908344
UBE2B_HUMAN	UBE2B	physical	10908344
UBE2A_HUMAN	UBE2A	physical	10884424
UBE2B_HUMAN	UBE2B	physical	10884424
RAD51_HUMAN	RAD51	physical	19396164
TP53B_HUMAN	TP53BP1	physical	19228710
FACD2_HUMAN	FANCD2	physical	21355096
FANCI_HUMAN	FANCI	physical	21355096
FACD2_HUMAN	FANCD2	physical	20967207
PCNA_HUMAN	PCNA	physical	20675655
CDC7_HUMAN	CDC7	physical	21098111
POLH_HUMAN	POLH	physical	21098111
UBE2B_HUMAN	UBE2B	physical	21422291
UBE2A_HUMAN	UBE2A	physical	21858012
UBE2B_HUMAN	UBE2B	physical	21858012
PCNA_HUMAN	PCNA	physical	21858012
H2A1A_HUMAN	HIST1H2AA	physical	21858012
PCNA_HUMAN	PCNA	physical	20600238
PCNA_HUMAN	PCNA	physical	20064529
NBN_HUMAN	NBN	physical	21884979
SLF1_HUMAN	ANKRD32	physical	22036607
PCNA_HUMAN	PCNA	physical	15359278
POLH_HUMAN	POLH	physical	15359278
HLTF_HUMAN	HLTF	physical	21396873
SHPRH_HUMAN	SHPRH	physical	21396873
SHPRH_MOUSE	Shprh	physical	21396873
RAD18_HUMAN	RAD18	physical	21396873
POLH_HUMAN	POLH	physical	21396873
POLK_HUMAN	POLK	physical	21396873
RAD18_HUMAN	RAD18	physical	21549715
UBE2B_HUMAN	UBE2B	physical	21549715
PCNA_HUMAN	PCNA	physical	17720710
UBE2B_HUMAN	UBE2B	physical	17720710
PCNA_HUMAN	PCNA	physical	21227930
SPRTN_HUMAN	SPRTN	physical	22681887
ORC2_HUMAN	ORC2	physical	22681887
PCNA_HUMAN	PCNA	physical	21967848
UBE2A_HUMAN	UBE2A	physical	18926833
RAD18_HUMAN	RAD18	physical	15509568
POL_HV1H2	gag-pol	physical	12016221
WRIP1_HUMAN	WRNIP1	physical	19556710
PCNA_HUMAN	PCNA	physical	17108083
UBE2A_HUMAN	UBE2A	physical	22456510
DPOLN_HUMAN	POLN	physical	22456510
RFC2_HUMAN	RFC2	physical	18245774
PCNA_HUMAN	PCNA	physical	18245774
SPRTN_HUMAN	SPRTN	physical	22902628
CBPD_HUMAN	CPD	physical	22902628
UBE2B_HUMAN	UBE2B	physical	20675655
UBE2A_HUMAN	UBE2A	physical	17108083
UBE2B_HUMAN	UBE2B	physical	18245774
UBE2B_HUMAN	UBE2B	physical	20064529
RL10A_HUMAN	RPL10A	physical	22939629
SLF1_MOUSE	Ankrd32	physical	15632077
POLH_HUMAN	POLH	physical	23345618
PCGF6_HUMAN	PCGF6	physical	22493164
TRIM8_HUMAN	TRIM8	physical	22493164
BRCA1_HUMAN	BRCA1	physical	23901102
DBF4A_HUMAN	DBF4	physical	24240236
UBP5_HUMAN	USP5	physical	24454762
LTP_EBVB9	BPLF1	physical	24672041
UBE2A_HUMAN	UBE2A	physical	24672041
RAD18_HUMAN	RAD18	physical	24672041
UBC_HUMAN	UBC	physical	17550899
SIVA_HUMAN	SIVA1	physical	24958773
PCNA_HUMAN	PCNA	physical	24958773
UBE2B_HUMAN	UBE2B	physical	24958773
SHPRH_HUMAN	SHPRH	physical	25023518
HLTF_HUMAN	HLTF	physical	25023518
RAD18_HUMAN	RAD18	physical	25023518
UBC_HUMAN	UBC	physical	25162118
PCNA_HUMAN	PCNA	physical	22904075
UBE2A_HUMAN	UBE2A	physical	22904075
UBC_HUMAN	UBC	physical	20935496
UBC_HUMAN	UBC	physical	22742833
UBC_HUMAN	UBC	physical	22343915
CREM_HUMAN	CREM	physical	26496610
HXK2_HUMAN	HK2	physical	26496610
ITSN1_HUMAN	ITSN1	physical	26496610
UBE2A_HUMAN	UBE2A	physical	26496610
SRGP3_HUMAN	SRGAP3	physical	26496610
TNPO3_HUMAN	TNPO3	physical	26496610
LIN7C_HUMAN	LIN7C	physical	26496610
SLF2_HUMAN	FAM178A	physical	26496610
SRGP1_HUMAN	SRGAP1	physical	26496610
ATPF1_HUMAN	ATPAF1	physical	26496610
SLF1_HUMAN	ANKRD32	physical	26496610
CAVN1_HUMAN	PTRF	physical	26496610
UBC_HUMAN	UBC	physical	25756347
UBP7_HUMAN	USP7	physical	25961918
PCNA_HUMAN	PCNA	physical	26170230
UBE2A_HUMAN	UBE2A	physical	26170230
REV1_MOUSE	Rev1	physical	26795561
UBC12_HUMAN	UBE2M	physical	28831681
PCNA_HUMAN	PCNA	physical	28831681
UBE2B_HUMAN	UBE2B	physical	27569044

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 RAD18_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-99; SER-103; SER-322 ANDSER-471, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-158; SER-164 ANDSER-471, AND MASS SPECTROMETRY.	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-99; SER-103; THR-118;SER-158 AND SER-164, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-107, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-471, ANDMASS SPECTROMETRY.	19007248 [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-403, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-409 AND SER-471,AND MASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND SER-471, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"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-99, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-471, AND MASSSPECTROMETRY.	15302935 [Abstract]