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UniProtKB/Swiss-Prot entry P49916


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNLI3_HUMAN
Primary accession number P49916
Secondary accession number Q16714
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 104)
Name and origin of the protein
Protein name DNA ligase 3
Synonyms EC 6.5.1.1
DNA ligase III
Polydeoxyribonucleotide synthase [ATP] 3
Gene name
Name: LIG3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Prostate;
PubMed=7760816 [NCBI, ExPASy, EBI, Israel, Japan]
Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A., Lindahl T.;
"Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination.";
Mol. Cell. Biol. 15:3206-3216(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
TISSUE=Testis;
PubMed=7565692 [NCBI, ExPASy, EBI, Israel, Japan]
Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S., Walter C.A., Schultz R.A., Besterman J.M., Husain I.;
"Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination.";
Mol. Cell. Biol. 15:5412-5422(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-780.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04689; PubMed=16625196 [NCBI, ExPASy, EBI, Israel, Japan]
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.";
Nature 440:1045-1049(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-155, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[10]
STRUCTURE BY NMR OF 837-922.
DOI=10.1006/prep.2001.1391; PubMed=11281714 [NCBI, ExPASy, EBI, Israel, Japan]
Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M., Thelen M.P., Cosman M.;
"Expression, purification, and biophysical characterization of the BRCT domain of human DNA ligase IIIalpha.";
Protein Expr. Purif. 21:401-411(2001).
[11]
STRUCTURE BY NMR OF 1-117.
DOI=10.1016/j.jmb.2004.06.035; PubMed=15288782 [NCBI, ExPASy, EBI, Israel, Japan]
Kulczyk A.W., Yang J.C., Neuhaus D.;
"Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha.";
J. Mol. Biol. 341:723-738(2004).
[12]
VARIANT [LARGE SCALE ANALYSIS] ASN-630.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X84740; CAA59230.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40671; AAA85022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF491645; AAL91592.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004223; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00000156; -.
IPI00029081; -.
PIR I37292; I37292.
RefSeq NP_002302.2; -.
NP_039269.2; -.
UniGene Hs.100299
3D structure databases
PDB
1IMO; NMR; -; A=837-922.[ExPASy / RCSB / EBI]
1IN1; NMR; -; A=837-922.[ExPASy / RCSB / EBI]
1UW0; NMR; -; A=1-117.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IMO; -.
1IN1; -.
1UW0; -.
ModBase P49916.
Protein-protein interaction databases
IntAct P49916; 7.
PTM databases
PhosphoSite P49916; -.
Enzyme and pathway databases
BRENDA 6.5.1.1; 247.
Reactome REACT_216; DNA Repair.
Organism-specific databases
GeneCards GC17P030331; -.
H-InvDB HIX0027160; -.
HGNC HGNC:6600; LIG3.
GenAtlas LIG3.
HPA HPA006723; -.
MIM 600940; gene. [NCBI / EBI]
PharmGKB PA30374; -.
Gene expression databases
ArrayExpress P49916; -.
Bgee P49916; -.
CleanEx HS_LIG3; -.
GermOnline ENSG00000005156; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0003910; Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from EC).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0006260; Biological process: DNA replication (inferred from electronic annotation from UniProtKB-KW).
GO:0007131; Biological process: reciprocal meiotic recombination (traceable author statement from ProtInc).
GO:0007283; Biological process: spermatogenesis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001357; BRCT.
IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
IPR001510; Znf_PARP.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
G3DSA:3.30.1740.10; Znf_PARP; 1.
Pfam PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
PF00645; zf-PARP; 1.
Pfam graphical view of domain structure.
ProDom PD004675; Znf_PolyADPpol; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00292; BRCT; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00574; dnl1; 1.
PROSITE PS50172; BRCT; 1.
PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PS00347; PARP_ZN_FINGER_1; 1.
PS50064; PARP_ZN_FINGER_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P49916; -.
Genome annotation databases
Ensembl ENSG00000005156; Homo sapiens. [Contig view]
GeneID 3980; -.
KEGG hsa:3980; -.
Phylogenomic databases
HOVERGEN P49916; -.
Other
DrugBank DB00290; Bleomycin.
NextBio 15598; -.
SOURCE LIG3; Homo sapiens.
ProtoNet P49916.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   922  922     DNA ligase 3. PRO_0000059574
DOMAIN   846   922  77     BRCT. 
ZN_FING   6    98  93     PARP-type. 
ACT_SITE   421   421        N6-AMP-lysine intermediate (By similarity). 
METAL   473   473        Magnesium 1 (By similarity). 
METAL   568   568        Magnesium 2 (By similarity). 
BINDING   419   419        ATP (By similarity). 
BINDING   426   426        ATP (By similarity). 
BINDING   441   441        ATP (By similarity). 
BINDING   573   573        ATP (By similarity). 
BINDING   584   584        ATP (By similarity). 
BINDING   588   588        ATP (By similarity). 
MOD_RES   122   122        Phosphothreonine (By similarity). 
MOD_RES   123   123        Phosphoserine. 
MOD_RES   140   140        Phosphoserine. 
MOD_RES   155   155        Phosphoserine. 
VAR_SEQ   846   922        VLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDM TSATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC -> RRPASEQRGRTVPAGRR (in isoform Beta). VSP_001302
VARIANT   137   137  1     R -> W (in dbSNP:rs3744356 [NCBI]). VAR_020196 
VARIANT   630   630  1     D -> N (in a colorectal cancer sample; somatic mutation). VAR_036513 
VARIANT   780   780  1     R -> H (in dbSNP:rs3136025 [NCBI]). VAR_018807 
VARIANT   811   811  1     K -> T (in dbSNP:rs4986974 [NCBI]). VAR_021938 
VARIANT   899   899  1     P -> S (in dbSNP:rs4986973 [NCBI]). VAR_020197 
STRAND   5    10  6      
STRAND   30    37  8      
HELIX   53    62  10      
STRAND   65    67  3      
STRAND   74    78  5      
TURN   79    81  3      
HELIX   84    98  15      
STRAND   101   103  3      
HELIX   837   840  4      
STRAND   849   851  3      
HELIX   865   875  11      
STRAND   891   893  3      
HELIX   906   915  10      
Sequence information
Length: 922 AA [This is the length of the unprocessed precursor] Molecular weight: 102691 Da [This is the MW of the unprocessed precursor] CRC64: FC3C60F988868808 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEQRFCVDY AKRGTAGCKK CKEKIVKGVC RIGKVVPNPF SESGGDMKEW YHIKCMFEKL 

        70         80         90        100        110        120 
ERARATTKKI EDLTELEGWE ELEDNEKEQI TQHIADLSSK AAGTPKKKAV VQAKLTTTGQ 

       130        140        150        160        170        180 
VTSPVKGASF VTSTNPRKFS GFSAKPNNSG EAPSSPTPKR SLSSSKCDPR HKDCLLREFR 

       190        200        210        220        230        240 
KLCAMVADNP SYNTKTQIIQ DFLRKGSAGD GFHGDVYLTV KLLLPGVIKT VYNLNDKQIV 

       250        260        270        280        290        300 
KLFSRIFNCN PDDMARDLEQ GDVSETIRVF FEQSKSFPPA AKSLLTIQEV DEFLLRLSKL 

       310        320        330        340        350        360 
TKEDEQQQAL QDIASRCTAN DLKCIIRLIK HDLKMNSGAK HVLDALDPNA YEAFKASRNL 

       370        380        390        400        410        420 
QDVVERVLHN AQEVEKEPGQ RRALSVQASL MTPVQPMLAE ACKSVEYAMK KCPNGMFSEI 

       430        440        450        460        470        480 
KYDGERVQVH KNGDHFSYFS RSLKPVLPHK VAHFKDYIPQ AFPGGHSMIL DSEVLLIDNK 

       490        500        510        520        530        540 
TGKPLPFGTL GVHKKAAFQD ANVCLFVFDC IYFNDVSLMD RPLCERRKFL HDNMVEIPNR 

       550        560        570        580        590        600 
IMFSEMKRVT KALDLADMIT RVIQEGLEGL VLKDVKGTYE PGKRHWLKVK KDYLNEGAMA 

       610        620        630        640        650        660 
DTADLVVLGA FYGQGSKGGM MSIFLMGCYD PGSQKWCTVT KCAGGHDDAT LARLQNELDM 

       670        680        690        700        710        720 
VKISKDPSKI PSWLKVNKIY YPDFIVPDPK KAAVWEITGA EFSKSEAHTA DGISIRFPRC 

       730        740        750        760        770        780 
TRIRDDKDWK SATNLPQLKE LYQLSKEKAD FTVVAGDEGS STTGGSSEEN KGPSGSAVSR 

       790        800        810        820        830        840 
KAPSKPSAST KKAEGKLSNS NSKDGNMQTA KPSAMKVGEK LATKSSPVKV GEKRKAADET 

       850        860        870        880        890        900 
LCQTKVLLDI FTGVRLYLPP STPDFSRLRR YFVAFDGDLV QEFDMTSATH VLGSRDKNPA 

       910        920 
AQQVSPEWIW ACIRKRRLVA PC 

P49916 in FASTA format

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