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Description:
Flap endonuclease 1 (EC 3.1.-.-) (Maturation factor 1) (MF1).
Molecular weight: 42593
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 ) double-strand break repair( GO:0006302 )
Important dates:
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
07-MAR-2006, entry version 56.
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 FEN1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X76771 | CAA54166.1 | - |
| EMBL | L37374 | AAA91331.1 | - |
| EMBL | AF523117 | AAM74238.1 | - |
| EMBL | AC004770 | AAC23394.1 | - |
| EMBL | BC000323 | AAH00323.1 | - |
| PIR | A56531 | A56531. | |
| PDB | 1UL1 | X-ray | X/Y/Z=2-380. |
| IntAct | P39748 | -.1 | |
| Ensembl | ENSG00000168496 | Homo sapiens.1 | |
| H-InvDB | HIX0009699 | -.1 | |
| HGNC | HGNC:3650 | FEN1.1 | |
| MIM | 600393 | gene. | |
| Reactome | P39748 | -.1 | |
| LinkHub | P39748 | -.1 | |
| GO | GO:0003684 | F:damaged DNA binding | TAS. |
| GO | GO:0003690 | F:double-stranded DNA binding | TAS. |
| GO | GO:0008309 | F:double-stranded DNA specific exodeoxyribonu... | TAS. |
| GO | GO:0004519 | F:endonuclease activity | TAS. |
| GO | GO:0004527 | F:exonuclease activity | TAS. |
| GO | GO:0006260 | P:DNA replication | NAS. |
| GO | GO:0006302 | P:double-strand break repair | TAS. |
| GO | GO:0048015 | P:phosphoinositide-mediated signaling | NAS. |
| GO | GO:0009650 | P:UV protection | TAS. |
| InterPro | IPR000513 | Exo_N_I. | |
| InterPro | IPR008918 | HhH2. | |
| InterPro | IPR006086 | XPG_I. | |
| InterPro | IPR006085 | XPG_N. | |
| InterPro | IPR006084 | XPGC_Rad. | |
| Pfam | PF00867 | XPG_I | 1. |
| Pfam | PF00752 | XPG_N | 1. |
| PRINTS | PR00853 | XPGRADSUPER. | |
| SMART | SM00279 | HhH2 | 1. |
| SMART | SM00484 | XPGI | 1. |
| SMART | SM00485 | XPGN | 1. |
| PROSITE | PS00841 | XPG_1 | 1. |
| PROSITE | PS00842 | XPG_2 | 1. |
Keywords:
3D-structure; Acetylation; Direct protein sequencing; Endonuclease; Hydrolase; Nuclear protein; Nuclease.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=94277093; PubMed=8007985;
RA Murray J.M., Tavassoli M., Al-Harithy R., Sheldrick K.S.,
RA Lehmann A.R., Carr A.M., Watts F.Z.;
RT "Structural and functional conservation of the human homolog of the
RT Schizosaccharomyces pombe rad2 gene, which is required for chromosome
RT segregation and recovery from DNA damage.";
RL Mol. Cell. Biol. 14:4878-4888(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lymphocyte;
RA Hiraoka L.R., Harrington J.J., Gerhard D.S., Lieber M.R., Hsieh C.-L.;
RT "Sequence of human FEN-1, a structure-specific endonuclease, and
RT chromosomal localization of the gene (FEN1) in mouse and human.";
RL Genomics 25:220-225(1995).
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 (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=95050647; PubMed=7961795;
RA Robins P., Pappin D.J., Wood R.D., Lindahl T.;
RT "Structural and functional homology between mammalian DNase IV and the
RT 5'-nuclease domain of Escherichia coli DNA polymerase I.";
RL J. Biol. Chem. 269:28535-28538(1994).
RN [7]
RP ACETYLATION.
RX PubMed=11430825; DOI=10.1016/S1097-2765(01)00272-6;
RA Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P.,
RA Hubscher U., Hottiger M.O.;
RT "Regulation of human flap endonuclease-1 activity by acetylation
RT through the transcriptional coactivator p300.";
RL Mol. Cell 7:1221-1231(2001).
RN [8]
RP INTERACTION WITH PCNA.
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).
Feature:
CHAIN 1 380 Flap endonuclease 1.
/FTId=PRO_0000154069.
REGION 1 104 N-domain.
REGION 122 253 I-domain.
REGION 328 355 Interaction with PCNA.
TURN 4 5
HELIX 6 11
TURN 12 13
TURN 15 16
STRAND 17 17
STRAND 20 21
HELIX 23 26
TURN 27 28
STRAND 31 34
HELIX 35 43
STRAND 44 44
HELIX 62 76
TURN 77 78
STRAND 81 85
STRAND 88 88
STRAND 91 91
STRAND 136 136
HELIX 138 148
TURN 149 149
STRAND 152 154
STRAND 156 157
HELIX 159 169
TURN 170 170
STRAND 171 176
STRAND 178 178
TURN 180 180
HELIX 181 184
TURN 185 186
STRAND 188 192
STRAND 194 195
STRAND 204 208
HELIX 209 216
TURN 217 217
HELIX 220 231
STRAND 233 235
TURN 239 240
HELIX 243 252
STRAND 253 255
HELIX 256 260
TURN 261 262
TURN 266 267
STRAND 268 268
STRAND 272 273
HELIX 276 284
STRAND 285 285
HELIX 291 293
HELIX 303 309
TURN 310 313
STRAND 314 314
HELIX 318 332
STRAND 333 333
STRAND 336 337
HELIX 340 343
STRAND 344 351
Comments:
-!- FUNCTION: Endonuclease that cleave the 5'overhanging flap
structure that is generated by displacement synthesis when DNA
polymerase encounters the 5'end of a downstream Okazaki fragment.
It fails to cleave other DNA structures, including 3'flaps and
single stranded DNA (By similarity).
-!- SUBUNIT: Interacts with PCNA.
-!- INTERACTION:
P54132:BLM; NbExp=3; IntAct=EBI-707816, EBI-621372;
P12004:PCNA; NbExp=1; IntAct=EBI-707816, EBI-358311;
Q14191:WRN; NbExp=7; IntAct=EBI-707816, EBI-368417;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Acetylated by p300.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily.
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Sequence length: 380
MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET
TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE
QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM
DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG
IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE
PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP
KGSTKKKAKT GAAGKFKRGK