Protein data for PCNA_HUMAN:

Description:
Proliferating cell nuclear antigen (PCNA) (Cyclin).

Molecular weight: 28769

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-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
07-FEB-2006, entry version 74.

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 PCNA_HUMAN:

DatabasePointerAdd. info#1Add. info#2
EMBLM15796AAA35736.1-
EMBLJ04718AAA60040.1-
EMBLAF527838AAM78556.1-
EMBLAL121924CAC27344.1-
EMBLBC000491AAH00491.1-
EMBLBC062439AAH62439.1-
PIRA27445WMHUET.
PDB1AXCX-rayA/C/E=1-261.
PDB1U76X-rayA/C/E=1-261.
PDB1U7BX-rayA=1-261.
PDB1UL1X-rayA/B/C=1-261.
PDB1VYJX-rayA/C/E/G/I/K=1-261.
PDB1VYMX-rayA/B/C=1-261.
PDB1W60X-rayA/B=1-261.
IntActP12004-.1
SWISS-2DPAGEP12004HUMAN.
EnsemblENSG00000132646Homo sapiens.1
H-InvDBHIX0015618-.1
HGNCHGNC:8729PCNA.1
MIM176740gene.
ReactomeP12004-.1
LinkHubP12004-.1
GOGO:0005660C:delta-DNA polymerase cofactor complexTAS.
GOGO:0008283P:cell proliferationTAS.
GOGO:0006281P:DNA repairNAS.
GOGO:0006260P:DNA replicationNAS.
GOGO:0048015P:phosphoinositide-mediated signalingNAS.
GOGO:0000074P:regulation of progression through cell cycleNAS.
InterProIPR000730Pr_cel_nuc_antig.
PANTHERPTHR11352Pr_cel_nuc_antig.11.
PfamPF02747PCNA_C1.
PfamPF00705PCNA_N1.
PIRSFPIRSF002090PCNA1.
PRINTSPR00339PCNACYCLIN.
ProDomPD002673Pr_cel_nuc_antig1.
TIGRFAMsTIGR00590pcna1.
PROSITEPS01251PCNA_11.
PROSITEPS00293PCNA_21.

General information about the databases mentioned above

Keywords:
3D-structure; Direct protein sequencing; DNA replication; DNA-binding; Nuclear protein; Systemic lupus erythematosus; Ubl conjugation.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX MEDLINE=87175520; PubMed=2882507;
RA Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H.,
RA Bravo R.;
RT "Cloning and sequence of the human nuclear protein cyclin: homology
RT with DNA-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=89214190; PubMed=2565339;
RA Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R.,
RA Calabretta B.;
RT "Structure of the human gene for the proliferating cell nuclear
RT antigen.";
RL J. Biol. Chem. 264:7466-7472(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Lung;
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 PROTEIN SEQUENCE OF 1-26.
RX MEDLINE=87173009; PubMed=2882422; DOI=10.1038/326471a0;
RA Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B.;
RT "The cell-cycle regulated proliferating cell nuclear antigen is
RT required for SV40 DNA replication in vitro.";
RL Nature 326:471-475(1987).
RN [7]
RP INTERACTION WITH ERCC5/XPG.
RX MEDLINE=97450983; PubMed=9305916; DOI=10.1074/jbc.272.39.24522;
RA Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.;
RT "The DNA repair endonuclease XPG binds to proliferating cell nuclear
RT antigen (PCNA) and shares sequence elements with the PCNA-binding
RT regions of FEN-1 and cyclin-dependent kinase inhibitor p21.";
RL J. Biol. Chem. 272:24522-24529(1997).
RN [8]
RP INTERACTION WITH DNMT1.
RX MEDLINE=97451025; PubMed=9302295; DOI=10.1126/science.277.5334.1996;
RA Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
RT "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
RT p21WAF1.";
RL Science 277:1996-2000(1997).
RN [9]
RP INTERACTION WITH CDC6.

RA Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M.,
RA Parvin J.D., Dutta A.;
RT "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is
RT selectively eliminated from the nucleus at the onset of S phase.";
RL Mol. Cell. Biol. 18:2758-2767(1998).
RN [10]
RP INTERACTION WITH APEX2.
RX MEDLINE=21270456; PubMed=11376153; DOI=10.1093/nar/29.11.2349;
RA Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M.,
RA Fujiwara T., Nakabeppu Y.;
RT "Human APE2 protein is mostly localized in the nuclei and to some
RT extent in the mitochondria, while nuclear APE2 is partly associated
RT with proliferating cell nuclear antigen.";
RL Nucleic Acids Res. 29:2349-2360(2001).
RN [11]
RP INTERACTION WITH POLK.
RX MEDLINE=21644468; PubMed=11784855;
RA Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J.,
RA Prakash L., Prakash S.;
RT "Stimulation of DNA synthesis activity of human DNA polymerase kappa
RT by PCNA.";
RL Mol. Cell. Biol. 22:784-791(2002).
RN [12]
RP INTERACTION WITH POLDIP2.
RC TISSUE=Placenta;
RX MEDLINE=22526690; PubMed=12522211; DOI=10.1074/jbc.M208694200;
RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
RT "Identification of a novel protein, PDIP38, that interacts with the
RT p50 subunit of DNA polymerase delta and proliferating cell nuclear
RT antigen.";
RL J. Biol. Chem. 278:10041-10047(2003).
RN [13]
RP INTERACTION WITH EXO1.
RX PubMed=15225546; DOI=10.1016/j.molcel.2004.06.016;
RA Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M.,
RA Modrich P.;
RT "A defined human system that supports bidirectional mismatch-provoked
RT excision.";
RL Mol. Cell 15:31-41(2004).
RN [14]
RP UBIQUITINATION, AND INTERACTION WITH POLH.
RX PubMed=15149598; DOI=10.1016/S1097-2765(04)00259-X;
RA Kannouche P.L., Wing J., Lehmann A.R.;
RT "Interaction of human DNA polymerase eta with monoubiquitinated PCNA:
RT a possible mechanism for the polymerase switch in response to DNA
RT damage.";
RL Mol. Cell 14:491-500(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX MEDLINE=97015085; PubMed=8861913; DOI=10.1016/S0092-8674(00)81347-1;
RA Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.;
RT "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with
RT human PCNA.";
RL Cell 87:297-306(1996).

Feature:
CHAIN 1 261 Proliferating cell nuclear antigen.
/FTId=PRO_0000149158.
DNA_BIND 61 80 Potential.
STRAND 2 7
TURN 9 9
HELIX 10 20
TURN 21 22
STRAND 24 31
TURN 32 33
STRAND 34 40
TURN 42 43
STRAND 44 53
HELIX 54 56
STRAND 57 64
STRAND 66 71
HELIX 72 79
TURN 80 81
STRAND 82 82
TURN 84 85
STRAND 87 92
TURN 94 95
STRAND 97 104
TURN 106 107
STRAND 108 109
STRAND 111 117
STRAND 127 127
STRAND 134 140
HELIX 141 152
TURN 153 154
STRAND 156 163
TURN 164 165
STRAND 166 173
TURN 174 175
STRAND 176 182
STRAND 193 193
STRAND 196 201
STRAND 203 208
HELIX 209 221
STRAND 223 229
TURN 231 232
STRAND 233 233
STRAND 235 241
TURN 242 244
STRAND 245 251
STRAND 254 254

Comments:
-!- FUNCTION: This protein is an auxiliary protein of DNA polymerase
delta and is involved in the control of eukaryotic DNA replication
by increasing the polymerase's processibility during elongation of
the leading strand.
-!- SUBUNIT: Homotrimer. Forms a complex with activator 1
heteropentamer in the presence of ATP. Interacts with POLH, POLK,
DNMT1, ERCC5/XPG, FEN1, CDC6, APEX2 and POLDIP2. Interacts with
EXO1.
-!- INTERACTION:
P39748:FEN1; NbExp=1; IntAct=EBI-358311, EBI-707816;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: DNA damage leads to monoubiquitination.
-!- DISEASE: Antibodies are present in sera from patients with
systemic lupus erythematosus.
-!- SIMILARITY: Belongs to the PCNA family.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------

Sequence length: 261

     MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL TLRSEGFDTY
     RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD
     LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSHIGDAVVI SCAKDGVKFS ASGELGNGNI
     KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK
     IADMGHLKYY LAPKIEDEEG S