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Description:
DNA ligase 3 (EC 6.5.1.1) (DNA ligase III) (Polydeoxyribonucleotidesynthase [ATP] 3).
Molecular weight: 10269
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-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-FEB-2006, entry version 62.
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 DNL3_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X84740 | CAA59230.1 | - |
| EMBL | U40671 | AAA85022.1 | - |
| EMBL | AF491645 | AAL91592.1 | - |
| PIR | I37292 | I37292. | |
| PDB | 1IMO | NMR | A=837-922. |
| PDB | 1IN1 | NMR | A=837-922. |
| PDB | 1UW0 | NMR | A=1-117. |
| Ensembl | ENSG00000005156 | Homo sapiens.1 | |
| HGNC | HGNC:6600 | LIG3.1 | |
| MIM | 600940 | gene. | |
| Reactome | P49916 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0003677 | F:DNA binding | TAS. |
| GO | GO:0003909 | F:DNA ligase activity | TAS. |
| GO | GO:0006281 | P:DNA repair | TAS. |
| GO | GO:0007131 | P:meiotic recombination | TAS. |
| GO | GO:0007283 | P:spermatogenesis | TAS. |
| InterPro | IPR001357 | BRCT. | |
| InterPro | IPR000977 | DNA_ligase. | |
| InterPro | IPR012309 | DNA_ligase_A_C. | |
| InterPro | IPR012310 | DNA_ligase_A_M. | |
| InterPro | IPR012308 | DNA_ligase_A_N. | |
| InterPro | IPR001510 | Znf_PARP. | |
| PANTHER | PTHR10459 | DNA_ligase.1 | 1. |
| Pfam | PF04679 | DNA_ligase_A_C | 1. |
| Pfam | PF01068 | DNA_ligase_A_M | 1. |
| Pfam | PF04675 | DNA_ligase_A_N | 1. |
| Pfam | PF00645 | zf-PARP | 1. |
| ProDom | PD004675 | Znf_PolyADPpol | 1. |
| SMART | SM00292 | BRCT | 1. |
| TIGRFAMs | TIGR00574 | dnl1 | 1. |
| PROSITE | PS50172 | BRCT | 1. |
| PROSITE | PS00697 | DNA_LIGASE_A1 | 1. |
| PROSITE | PS00333 | DNA_LIGASE_A2 | 1. |
| PROSITE | PS50160 | DNA_LIGASE_A3 | 1. |
| PROSITE | PS00347 | PARP_ZN_FINGER_1 | 1. |
| PROSITE | PS50064 | PARP_ZN_FINGER_2 | 1. |
Keywords:
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Metal-binding; Nuclear protein; Nucleotide-binding; Polymorphism; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Prostate;
RX MEDLINE=95280920; PubMed=7760816;
RA Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C.,
RA Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E.,
RA Haseltine W.A., Lindahl T.;
RT "Molecular cloning and expression of human cDNAs encoding a novel DNA
RT ligase IV and DNA ligase III, an enzyme active in DNA repair and
RT recombination.";
RL Mol. Cell. Biol. 15:3206-3216(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM BETA).
RC TISSUE=Testis;
RX MEDLINE=96009568; PubMed=7565692;
RA Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S.,
RA Walter C.A., Schultz R.A., Besterman J.M., Husain I.;
RT "Mammalian DNA ligase III: molecular cloning, chromosomal
RT localization, and expression in spermatocytes undergoing meiotic
RT recombination.";
RL Mol. Cell. Biol. 15:5412-5422(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-780.
RA Rieder M.J., Braun A.C., Montoya M.A., Chung M.-W., Nguyen C.P.,
RA Nguyen D.A., Livingston R.J., 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 (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP STRUCTURE BY NMR OF 837-922.
RX PubMed=11281714; DOI=10.1006/prep.2001.1391;
RA Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M.,
RA Thelen M.P., Cosman M.;
RT "Expression, purification, and biophysical characterization of the
RT BRCT domain of human DNA ligase IIIalpha.";
RL Protein Expr. Purif. 21:401-411(2001).
Feature:
CHAIN 1 922 DNA ligase 3.
/FTId=PRO_0000059574.
DOMAIN 846 922 BRCT.
ZN_FING 6 98 PARP-type.
ACT_SITE 421 421 N6-AMP-lysine intermediate (By
similarity).
VARSPLIC 846 922 VLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMT
SATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC -> R
RPASEQRGRTVPAGRR (in isoform Beta).
/FTId=VSP_001302.
VARIANT 137 137 R -> W (in dbSNP:3744356).
/FTId=VAR_020196.
VARIANT 780 780 R -> H (in dbSNP:3136025).
/FTId=VAR_018807.
VARIANT 811 811 K -> T (in dbSNP:4986974).
/FTId=VAR_021938.
VARIANT 899 899 P -> S (in dbSNP:4986973).
/FTId=VAR_020197.
STRAND 5 10
STRAND 13 14
STRAND 16 17
TURN 19 20
STRAND 21 22
STRAND 24 25
TURN 27 28
STRAND 30 37
TURN 39 40
STRAND 42 43
STRAND 46 47
STRAND 50 50
HELIX 53 62
STRAND 63 63
STRAND 65 67
STRAND 70 70
TURN 72 73
STRAND 74 78
TURN 79 81
STRAND 82 82
HELIX 84 98
STRAND 101 103
STRAND 108 108
HELIX 837 840
TURN 841 842
STRAND 843 843
TURN 844 845
STRAND 849 851
TURN 852 853
STRAND 855 855
TURN 860 861
STRAND 862 862
TURN 863 864
HELIX 865 875
STRAND 876 876
STRAND 878 878
TURN 882 883
TURN 886 887
STRAND 891 893
TURN 896 897
TURN 899 900
STRAND 901 901
STRAND 903 904
HELIX 906 915
STRAND 916 917
Comments:
-!- FUNCTION: Interacts with DNA-repair protein XRCC1 and can correct
defective DNA strand-break repair and sister chromatid exchange
following treatment with ionizing radiation and alkylating agents.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
(deoxyribonucleotide)(m) = AMP + diphosphate +
(deoxyribonucleotide)(n+m).
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=P49916-1; Sequence=Displayed;
Name=Beta;
IsoId=P49916-2; Sequence=VSP_001302;
-!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
-!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
-!- SIMILARITY: Contains 1 BRCT domain.
-!- SIMILARITY: Contains 1 PARP-type zinc finger.
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Sequence length: 922
MAEQRFCVDY AKRGTAGCKK CKEKIVKGVC RIGKVVPNPF SESGGDMKEW YHIKCMFEKL
ERARATTKKI EDLTELEGWE ELEDNEKEQI TQHIADLSSK AAGTPKKKAV VQAKLTTTGQ
VTSPVKGASF VTSTNPRKFS GFSAKPNNSG EAPSSPTPKR SLSSSKCDPR HKDCLLREFR
KLCAMVADNP SYNTKTQIIQ DFLRKGSAGD GFHGDVYLTV KLLLPGVIKT VYNLNDKQIV
KLFSRIFNCN PDDMARDLEQ GDVSETIRVF FEQSKSFPPA AKSLLTIQEV DEFLLRLSKL
TKEDEQQQAL QDIASRCTAN DLKCIIRLIK HDLKMNSGAK HVLDALDPNA YEAFKASRNL
QDVVERVLHN AQEVEKEPGQ RRALSVQASL MTPVQPMLAE ACKSVEYAMK KCPNGMFSEI
KYDGERVQVH KNGDHFSYFS RSLKPVLPHK VAHFKDYIPQ AFPGGHSMIL DSEVLLIDNK
TGKPLPFGTL GVHKKAAFQD ANVCLFVFDC IYFNDVSLMD RPLCERRKFL HDNMVEIPNR
IMFSEMKRVT KALDLADMIT RVIQEGLEGL VLKDVKGTYE PGKRHWLKVK KDYLNEGAMA
DTADLVVLGA FYGQGSKGGM MSIFLMGCYD PGSQKWCTVT KCAGGHDDAT LARLQNELDM
VKISKDPSKI PSWLKVNKIY YPDFIVPDPK KAAVWEITGA EFSKSEAHTA DGISIRFPRC
TRIRDDKDWK SATNLPQLKE LYQLSKEKAD FTVVAGDEGS STTGGSSEEN KGPSGSAVSR
KAPSKPSAST KKAEGKLSNS NSKDGNMQTA KPSAMKVGEK LATKSSPVKV GEKRKAADET
LCQTKVLLDI FTGVRLYLPP STPDFSRLRR YFVAFDGDLV QEFDMTSATH VLGSRDKNPA
AQQVSPEWIW ACIRKRRLVA PC