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RFC3

Protein FULL name:

Replication factor C subunit 3, Activator 1 subunit 3, Replication factor C 38 kDa subunit, Activator 1 38 kDa subunit,


Protein SHORT name:

RF-C 38 kDa subunit RFC38 A1 38 kDa subunit.


RFC3 (Homo sapiens) is product of expression of RFC3 gene.


RFC3 is involved in:

DDS in Homo sapiens
     





FUNCTION: 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.

SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA.

INTERACTION: P35249:RFC4; NbExp=1; IntAct=EBI-1055010, EBI-476655;

SUBCELLULAR LOCATION: Nucleus (Probable).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

SIMILARITY: Belongs to the activator 1 small subunits family.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


This protein can be a part of a given complexes:
NCBI GenPept GI number(s): 3915601
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P40938 P40938
PFAM: PF00004
PF10424
PF00004
PF10424
InterPro: IPR003593
IPR003959
IPR008921
IPR019483
IPR003593
IPR003959
IPR008921
IPR019483
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSLWVDKYRPCSLGRLDYHKEQAAQLRNLVQCGDFPHLLVYGPSGAGKKT
RIMCILRELYGVGVEKLRIEHQTITTPSKKKIEISTIASNYHLEVNPSDA
GNSDRVVIQEMLKTVAQSQQLETNSQRDFKVVLLTEVDKLTKDAQHALRR
TMEKYMSTCRLILCCNSTSKVIPPIRSRCLAVRVPAPSIEDICHVLSTVC
KKEGLNLPSQLAHRLAEKSCRNLRKALLMCEACRVQQYPFTADQEIPETD
WEVYLRETANAIVSQQTPQRLLEVRGRLYELLTHCIPPEIIMKGLLSELL
HNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKKFMEDG
LEGMMF

RFC3 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Homology in accessory proteins of replicative polymerases--E. coli to humans. O'Donnell M, Onrust R, Dean FB, Chen M, Hurwitz J Nucleic Acids Res Feb. 11, 1993
The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. Rauen M, Burtelow MA, Dufault VM, Karnitz LM J Biol Chem Sept. 22, 2000
Purification and characterization of human DNA damage checkpoint Rad complexes. Lindsey-Boltz LA, Bermudez VP, Hurwitz J, Sancar A Proc Natl Acad Sci U S A Sept. 25, 2001
The DNA sequence and analysis of human chromosome 13. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT Nature April 1, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009


Last modification of this entry: Oct. 6, 2010.

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