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RFC4

Protein FULL name:

Replication factor C subunit 4, Activator 1 subunit 4, Replication factor C 37 kDa subunit, Activator 1 37 kDa subunit,


Protein SHORT name:

RF-C 37 kDa subunit RFC37 A1 37 kDa subunit.


RFC4 (Homo sapiens) is product of expression of RFC4 gene.


RFC4 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. This subunit may be involved in the elongation of the multiprimed DNA template.

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: P35250:RFC2; NbExp=2; IntAct=EBI-476655, EBI-476409; P40938:RFC3; NbExp=1; IntAct=EBI-476655, EBI-1055010;

SUBCELLULAR LOCATION: Nucleus (Probable).

MISCELLANEOUS: Despite of the presence of a putative ATP-binding motif, this protein does not bind ATP.

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): 1703052
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P35249 P35249
PFAM: PF00004
PF08542
PF00004
PF08542
InterPro: IPR003593
IPR003959
IPR008921
IPR013748
IPR003593
IPR003959
IPR008921
IPR013748
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MQAFLKGTSISTKPPLTKDRGVAASAGSSGENKKAKPVPWVEKYRPKCVD
EVAFQEEVVAVLKKSLEGADLPNLLFYGPPGTGKTSTILAAARELFGPEL
FRLRVLELNASDERGIQVVREKVKNFAQLTVSGSRSDGKPCPPFKIVILD
EADSMTSAAQAALRRTMEKESKTTRFCLICNYVSRIIEPLTSRCSKFRFK
PLSDKIQQQRLLDIAKKENVKISDEGIAYLVKVSEGDLRKAITFLQSATR
LTGGKEITEKVITDIAGVIPAEKIDGVFAACQSGSFDKLEAVVKDLIDEG
HAATQLVNQLHDVVVENNLSDKQKSIITEKLAEVDKCLADGADEHLQLIS
LCATVMQQLSQNC

RFC4 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Studies of the cloned 37-kDa subunit of activator 1 (replication factor C) of HeLa cells. Chen M, Pan ZQ, Hurwitz J Proc Natl Acad Sci U S A June 15, 1992
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 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
The consensus coding sequences of human breast and colorectal cancers. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE Science Oct. 13, 2006
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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