dbPTM

RFC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RFC3_HUMAN
UniProt AC	P40938
Protein Name	Replication factor C subunit 3
Gene Name	RFC3
Organism	Homo sapiens (Human).
Sequence Length	356
Subcellular Localization	Nucleus .
Protein Description	The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1..
Protein Sequence	MSLWVDKYRPCSLGRLDYHKEQAAQLRNLVQCGDFPHLLVYGPSGAGKKTRIMCILRELYGVGVEKLRIEHQTITTPSKKKIEISTIASNYHLEVNPSDAGNSDRVVIQEMLKTVAQSQQLETNSQRDFKVVLLTEVDKLTKDAQHALRRTMEKYMSTCRLILCCNSTSKVIPPIRSRCLAVRVPAPSIEDICHVLSTVCKKEGLNLPSQLAHRLAEKSCRNLRKALLMCEACRVQQYPFTADQEIPETDWEVYLRETANAIVSQQTPQRLLEVRGRLYELLTHCIPPEIIMKGLLSELLHNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKKFMEDGLEGMMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLWVDKYR ------CCCCCCCCC	30.82	26552605
7	Trimethylation	-MSLWVDKYRPCSLG -CCCCCCCCCCCCCC	33.27	-
7	Ubiquitination	-MSLWVDKYRPCSLG -CCCCCCCCCCCCCC	33.27	-
7	Methylation	-MSLWVDKYRPCSLG -CCCCCCCCCCCCCC	33.27	23644510
7	Acetylation	-MSLWVDKYRPCSLG -CCCCCCCCCCCCCC	33.27	25953088
8	Phosphorylation	MSLWVDKYRPCSLGR CCCCCCCCCCCCCCC	18.47	26552605
12	Phosphorylation	VDKYRPCSLGRLDYH CCCCCCCCCCCCCCC	36.22	23401153
20	Acetylation	LGRLDYHKEQAAQLR CCCCCCCHHHHHHHH	45.34	19608861
20	Ubiquitination	LGRLDYHKEQAAQLR CCCCCCCHHHHHHHH	45.34	21906983
41	Phosphorylation	DFPHLLVYGPSGAGK CCCEEEEECCCCCCH	24.24	29496907
48	Ubiquitination	YGPSGAGKKTRIMCI ECCCCCCHHHHHHHH	50.90	-
48	Acetylation	YGPSGAGKKTRIMCI ECCCCCCHHHHHHHH	50.90	26051181
49	Ubiquitination	GPSGAGKKTRIMCIL CCCCCCHHHHHHHHH	41.96	-
60	Phosphorylation	MCILRELYGVGVEKL HHHHHHHHCCCCCEE	12.66	20068231
66	Ubiquitination	LYGVGVEKLRIEHQT HHCCCCCEEEEEEEE	40.43	21890473
66	2-Hydroxyisobutyrylation	LYGVGVEKLRIEHQT HHCCCCCEEEEEEEE	40.43	-
66	Ubiquitination	LYGVGVEKLRIEHQT HHCCCCCEEEEEEEE	40.43	21890473
66	Acetylation	LYGVGVEKLRIEHQT HHCCCCCEEEEEEEE	40.43	25953088
73	Phosphorylation	KLRIEHQTITTPSKK EEEEEEEEEECCCCC	23.38	27732954
75	Phosphorylation	RIEHQTITTPSKKKI EEEEEEEECCCCCCE	35.72	30576142
76	Phosphorylation	IEHQTITTPSKKKIE EEEEEEECCCCCCEE	23.01	28985074
78	Phosphorylation	HQTITTPSKKKIEIS EEEEECCCCCCEEEE	55.82	27732954
79	Acetylation	QTITTPSKKKIEIST EEEECCCCCCEEEEE	60.33	25953088
79	Ubiquitination	QTITTPSKKKIEIST EEEECCCCCCEEEEE	60.33	-
91	Phosphorylation	ISTIASNYHLEVNPS EEEECCCEEEECCHH	12.80	20068231
98	Phosphorylation	YHLEVNPSDAGNSDR EEEECCHHHCCCCCH	34.58	20068231
111	Sulfoxidation	DRVVIQEMLKTVAQS CHHHHHHHHHHHHHH	2.39	21406390
113	Ubiquitination	VVIQEMLKTVAQSQQ HHHHHHHHHHHHHHH	39.38	21906983
114	Phosphorylation	VIQEMLKTVAQSQQL HHHHHHHHHHHHHHH	19.67	29083192
118	Phosphorylation	MLKTVAQSQQLETNS HHHHHHHHHHHCCCC	15.34	29083192
123	Phosphorylation	AQSQQLETNSQRDFK HHHHHHCCCCCCCCE	49.08	-
125	Phosphorylation	SQQLETNSQRDFKVV HHHHCCCCCCCCEEE	33.73	17525332
130	Ubiquitination	TNSQRDFKVVLLTEV CCCCCCCEEEEEEEH	35.40	-
139	Ubiquitination	VLLTEVDKLTKDAQH EEEEEHHHHHHHHHH	64.33	21890473
139	Acetylation	VLLTEVDKLTKDAQH EEEEEHHHHHHHHHH	64.33	26051181
142	Ubiquitination	TEVDKLTKDAQHALR EEHHHHHHHHHHHHH	62.60	-
154	Ubiquitination	ALRRTMEKYMSTCRL HHHHHHHHHHCCCCE	35.12	-
154	Acetylation	ALRRTMEKYMSTCRL HHHHHHHHHHCCCCE	35.12	25953088
167	Phosphorylation	RLILCCNSTSKVIPP CEEEECCCCCCCCCC	21.83	24043423
168	Phosphorylation	LILCCNSTSKVIPPI EEEECCCCCCCCCCC	20.69	24043423
169	Phosphorylation	ILCCNSTSKVIPPIR EEECCCCCCCCCCCH	25.42	24043423
170	Ubiquitination	LCCNSTSKVIPPIRS EECCCCCCCCCCCHH	44.25	-
197	Phosphorylation	EDICHVLSTVCKKEG HHHHHHHHHHHHHCC	20.08	22210691
198	Phosphorylation	DICHVLSTVCKKEGL HHHHHHHHHHHHCCC	26.26	22210691
201	Acetylation	HVLSTVCKKEGLNLP HHHHHHHHHCCCCCC	49.91	25953088
201	Ubiquitination	HVLSTVCKKEGLNLP HHHHHHHHHCCCCCC	49.91	-
202	Ubiquitination	VLSTVCKKEGLNLPS HHHHHHHHCCCCCCH	52.46	21890473
202	Ubiquitination	VLSTVCKKEGLNLPS HHHHHHHHCCCCCCH	52.46	21890473
209	Phosphorylation	KEGLNLPSQLAHRLA HCCCCCCHHHHHHHH	40.78	22210691
218	Ubiquitination	LAHRLAEKSCRNLRK HHHHHHHHHHHHHHH	49.61	-
225	Ubiquitination	KSCRNLRKALLMCEA HHHHHHHHHHHHHHH	46.69	-
264	Phosphorylation	ETANAIVSQQTPQRL HHHHHHHCCCCHHHH	15.51	28555341
279	Phosphorylation	LEVRGRLYELLTHCI HHHHHHHHHHHHHCC	11.81	29496907
283	Phosphorylation	GRLYELLTHCIPPEI HHHHHHHHHCCCHHH	27.59	26270265
308	Ubiquitination	HNCDGQLKGEVAQMA HCCCCCCHHHHHHHH	45.17	-
343	Phosphorylation	VAKFMALYKKFMEDG HHHHHHHHHHHHHHC	11.55	-
344	Ubiquitination	AKFMALYKKFMEDGL HHHHHHHHHHHHHCC	40.14	-

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
Oops, there are no upstream regulatory protein records of RFC3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RFC3_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 RFC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	12766176
CTF18_HUMAN	CHTF18	physical	12766176
RFC4_HUMAN	RFC4	physical	9488738
RFC1_HUMAN	RFC1	physical	9488738
RFC4_HUMAN	RFC4	physical	8692848
RFC1_HUMAN	RFC1	physical	8692848
RFC4_HUMAN	RFC4	physical	22939629
RFC5_HUMAN	RFC5	physical	22939629
RFC2_HUMAN	RFC2	physical	26344197
RFC4_HUMAN	RFC4	physical	26344197
RFC5_HUMAN	RFC5	physical	26344197

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 RFC3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-125, AND MASSSPECTROMETRY.	17525332 [Abstract]