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Protein data for RFC4_HUMAN:

Description:
Activator 1 37 kDa subunit (Replication factor C 37 kDa subunit) (A137 kDa subunit) (RF-C 37 kDa subunit) (RFC37).

Molecular weight: 39682

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
07-MAR-2006, entry version 57.

Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein RFC4_HUMAN:

DatabasePointerAdd. info#1Add. info#2
EMBLM87339AAB09785.1-
EMBLAF538718AAM97933.1-
EMBLBT006987AAP35633.1-
EMBLBC017452AAH17452.1-
EMBLBC024022AAH24022.1-
HSSPQ9P9H21IQP
IntActP35249-.1
EnsemblENSG00000163918Homo sapiens.1
H-InvDBHIX0003934-.1
HGNCHGNC:9972RFC4.1
MIM102577gene.
ReactomeP35249-.1
GOGO:0005660C:delta-DNA polymerase cofactor complexTAS.
GOGO:0005663C:DNA replication factor C complexTAS.
GOGO:0005515F:protein bindingIPI.
GOGO:0006281P:DNA repairNAS.
GOGO:0006260P:DNA replicationNAS.
GOGO:0006271P:DNA strand elongationTAS.
GOGO:0048015P:phosphoinositide-mediated signalingNAS.
InterProIPR003593AAA_ATPase.
InterProIPR003959AAA_ATPase_centr.
InterProIPR000862RFC.
PfamPF00004AAA1.
SMARTSM00382AAA1.

General information about the databases mentioned above

Keywords:
ATP-binding; Direct protein sequencing; DNA replication; Nuclear protein; Nucleotide-binding; Polymorphism.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=92302215; PubMed=1351677;
RA Chen M., Pan Z.-Q., Hurwitz J.;
RT "Studies of the cloned 37-kDa subunit of activator 1 (replication
RT factor C) of HeLa cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5211-5215(1992).
RN [2]
RP SEQUENCE REVISION.
RA Hurwitz J.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-292.
RA Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W.,
RA Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP INTERACTION WITH RAD17.
RX MEDLINE=21457323; PubMed=11572977; DOI=10.1073/pnas.201373498;
RA Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.;
RT "Purification and characterization of human DNA damage checkpoint Rad
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001).

Feature:
CHAIN 1 363 Activator 1 37 kDa subunit.
/FTId=PRO_0000121757.
NP_BIND 78 85 ATP (Potential).
VARIANT 292 292 V -> A (in dbSNP:2066497).
/FTId=VAR_014307.

Comments:
-!- 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. The 37
kDa subunit may be involved in the elongation of the multiprimed
DNA template.
-!- SUBUNIT: Heterotetramer of subunits of 40, 38, 37, and 36.5 kDa
that can form a complex either with a fifth 140/145 kDa unit, 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;
-!- 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.
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Sequence length: 363

     MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD EVAFQEEVVA
     VLKKSLEGAD LPNLLFYGPP GTGKTSTILA AARELFGPEL FRLRVLELNA SDERGIQVVR
     EKVKNFAQLT VSGSRSDGKP CPPFKIVILD EADSMTSAAQ AALRRTMEKE SKTTRFCLIC
     NYVSRIIEPL TSRCSKFRFK PLSDKIQQQR LLDIAKKENV KISDEGIAYL VKVSEGDLRK
     AITFLQSATR LTGGKEITEK VITDIAGVIP AEKIDGVFAA CQSGSFDKLE AVVKDLIDEG
     HAATQLVNQL HDVVVENNLS DKQKSIITEK LAEVDKCLAD GADEHLQLIS LCATVMQQLS
     QNC

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