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DNA polymerase lambda (Pol Lambda) (EC 2.7.7.7) (EC 4.2.99.-) (DNA polymerase beta-2) (Pol beta2) (DNA polymerase kappa)

 DPOLL_HUMAN             Reviewed;         575 AA.
Q9UGP5; D3DR76; Q5JQP5; Q6NUM2; Q9BTN8; Q9HA10; Q9HB35;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 175.
RecName: Full=DNA polymerase lambda {ECO:0000305};
Short=Pol Lambda {ECO:0000305};
EC=2.7.7.7 {ECO:0000269|PubMed:10887191, ECO:0000269|PubMed:10982892, ECO:0000269|PubMed:12809503, ECO:0000269|PubMed:14627824, ECO:0000269|PubMed:15537631, ECO:0000269|PubMed:19806195};
EC=4.2.99.- {ECO:0000269|PubMed:11457865, ECO:0000269|PubMed:19806195};
AltName: Full=DNA polymerase beta-2 {ECO:0000303|PubMed:10887191};
Short=Pol beta2 {ECO:0000303|PubMed:10887191};
AltName: Full=DNA polymerase kappa {ECO:0000303|Ref.1};
Name=POLL {ECO:0000312|HGNC:HGNC:9184};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Garcia M., Dominguez O., Saniger M.L., Garcia M.J., Martinez C.,
Bernad A., Blanco L.;
"DNA polymerase kappa, a new mammalian meiotic polymerase.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
ACTIVITY.
TISSUE=Lymph node;
PubMed=10982892; DOI=10.1093/nar/28.18.3684;
Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S.,
Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.;
"Two novel human and mouse DNA polymerases of the polX family.";
Nucleic Acids Res. 28:3684-3693(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND SUBCELLULAR LOCATION.
PubMed=10887191; DOI=10.1074/jbc.M004263200;
Nagasawa K.I., Kitamura K., Yasui A., Nimura Y., Ikeda K., Hirai M.,
Matsukage A., Nakanishi M.;
"Identification and characterization of human DNA polymerase beta 2, a
DNA polymerase beta-related enzyme.";
J. Biol. Chem. 275:31233-31238(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-438.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-575 (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-312, AND ACTIVE SITE.
PubMed=11457865; DOI=10.1074/jbc.M106336200;
Garcia-Diaz M., Bebenek K., Kunkel T.A., Blanco L.;
"Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase
activity in human DNA polymerase lambda: a possible role in base
excision repair.";
J. Biol. Chem. 276:34659-34663(2001).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=12809503; DOI=10.1021/bi034198m;
Blanca G., Shevelev I., Ramadan K., Villani G., Spadari S.,
Huebscher U., Maga G.;
"Human DNA polymerase lambda diverged in evolution from DNA polymerase
beta toward specific Mn(++) dependence: a kinetic and thermodynamic
study.";
Biochemistry 42:7467-7476(2003).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-505 AND PHE-506.
PubMed=14627824; DOI=10.1093/nar/gkg896;
Shevelev I., Blanca G., Villani G., Ramadan K., Spadari S.,
Huebscher U., Maga G.;
"Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505
and Phe506 for both DNA polymerase and terminal transferase
activities.";
Nucleic Acids Res. 31:6916-6925(2003).
[12]
INTERACTION WITH PCNA.
PubMed=15358682; DOI=10.1096/fj.04-2268fje;
Maga G., Blanca G., Shevelev I., Frouin I., Ramadan K., Spadari S.,
Villani G., Huebscher U.;
"The human DNA polymerase lambda interacts with PCNA through a domain
important for DNA primer binding and the interaction is inhibited by
p21/WAF1/CIP1.";
FASEB J. 18:1743-1745(2004).
[13]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15537631; DOI=10.1074/jbc.M411650200;
Maga G., Ramadan K., Locatelli G.A., Shevelev I., Spadari S.,
Hubscher U.;
"DNA elongation by the human DNA polymerase lambda polymerase and
terminal transferase activities are differentially coordinated by
proliferating cell nuclear antigen and replication protein A.";
J. Biol. Chem. 280:1971-1981(2005).
[14]
FUNCTION, CATALYTIC ACTIVITY, VARIANT TRP-438, CHARACTERIZATION OF
VARIANT TRP-438, AND MUTAGENESIS OF ASP-427 AND ASP-429.
PubMed=19806195; DOI=10.1371/journal.pone.0007290;
Terrados G., Capp J.P., Canitrot Y., Garcia-Diaz M., Bebenek K.,
Kirchhoff T., Villanueva A., Boudsocq F., Bergoglio V., Cazaux C.,
Kunkel T.A., Hoffmann J.S., Blanco L.;
"Characterization of a natural mutator variant of human DNA polymerase
lambda which promotes chromosomal instability by compromising NHEJ.";
PLoS ONE 4:E7290-E7290(2009).
[15]
FUNCTION, AND CHARACTERIZATION OF VARIANT TRP-438.
PubMed=20693240; DOI=10.1093/carcin/bgq166;
Capp J.P., Boudsocq F., Bergoglio V., Trouche D., Cazaux C.,
Blanco L., Hoffmann J.S., Canitrot Y.;
"The R438W polymorphism of human DNA polymerase lambda triggers
cellular sensitivity to camptothecin by compromising the homologous
recombination repair pathway.";
Carcinogenesis 31:1742-1747(2010).
[16]
STRUCTURE BY NMR OF 241-327.
PubMed=12911298; DOI=10.1021/bi034298s;
DeRose E.F., Kirby T.W., Mueller G.A., Bebenek K., Garcia-Diaz M.,
Blanco L., Kunkel T.A., London R.E.;
"Solution structure of the lyase domain of human DNA polymerase
lambda.";
Biochemistry 42:9564-9574(2003).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 245-575 IN COMPLEX WITH
GAPPED DNA.
PubMed=14992725; DOI=10.1016/S1097-2765(04)00061-9;
Garcia-Diaz M., Bebenek K., Krahn J.M., Blanco L., Kunkel T.A.,
Pedersen L.C.;
"A structural solution for the DNA polymerase lambda-dependent repair
of DNA gaps with minimal homology.";
Mol. Cell 13:561-572(2004).
[18]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 242-575 IN COMPLEX WITH
MANGANESE AND DCTP.
PubMed=17475573; DOI=10.1016/j.dnarep.2007.03.005;
Garcia-Diaz M., Bebenek K., Krahn J.M., Pedersen L.C., Kunkel T.A.;
"Role of the catalytic metal during polymerization by DNA polymerase
lambda.";
DNA Repair 6:1333-1340(2007).
-!- FUNCTION: DNA polymerase that functions in several pathways of DNA
repair (PubMed:11457865, PubMed:19806195, PubMed:20693240).
Involved in base excision repair (BER) responsible for repair of
lesions that give rise to abasic (AP) sites in DNA
(PubMed:11457865, PubMed:19806195). Also contributes to DNA
double-strand break repair by non-homologous end joining and
homologous recombination (PubMed:19806195, PubMed:20693240). Has
both template-dependent and template-independent (terminal
transferase) DNA polymerase activities (PubMed:10982892,
PubMed:10887191, PubMed:12809503, PubMed:14627824,
PubMed:15537631, PubMed:19806195). Has also a 5'-deoxyribose-5-
phosphate lyase (dRP lyase) activity (PubMed:11457865,
PubMed:19806195). {ECO:0000269|PubMed:10887191,
ECO:0000269|PubMed:10982892, ECO:0000269|PubMed:11457865,
ECO:0000269|PubMed:12809503, ECO:0000269|PubMed:14627824,
ECO:0000269|PubMed:15537631, ECO:0000269|PubMed:19806195,
ECO:0000269|PubMed:20693240}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000269|PubMed:10887191,
ECO:0000269|PubMed:10982892, ECO:0000269|PubMed:12809503,
ECO:0000269|PubMed:14627824, ECO:0000269|PubMed:15537631,
ECO:0000269|PubMed:19806195}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17475573};
-!- SUBUNIT: Binds PCNA. {ECO:0000269|PubMed:14992725}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-10320765, EBI-10175124;
A1L4K1:FSD2; NbExp=4; IntAct=EBI-10320765, EBI-5661036;
Q6A162:KRT40; NbExp=3; IntAct=EBI-10320765, EBI-10171697;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-10320765, EBI-10172290;
P43365:MAGEA12; NbExp=5; IntAct=EBI-10320765, EBI-749530;
P23508:MCC; NbExp=4; IntAct=EBI-10320765, EBI-307531;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-10320765, EBI-302345;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-10320765, EBI-2212028;
Q12800:TFCP2; NbExp=3; IntAct=EBI-10320765, EBI-717422;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-10320765, EBI-1105213;
P36406:TRIM23; NbExp=3; IntAct=EBI-10320765, EBI-740098;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10887191}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UGP5-1; Sequence=Displayed;
Name=2;
IsoId=Q9UGP5-2; Sequence=VSP_056540, VSP_056541;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in
testis.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB14050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/poll/";
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EMBL; AJ131890; CAB65074.1; -; mRNA.
EMBL; AF161019; AAF27541.1; -; mRNA.
EMBL; AF283478; AAG22519.1; -; mRNA.
EMBL; AF525924; AAM77696.1; -; Genomic_DNA.
EMBL; AL627424; CAI41032.1; -; Genomic_DNA.
EMBL; CH471066; EAW49759.1; -; Genomic_DNA.
EMBL; CH471066; EAW49760.1; -; Genomic_DNA.
EMBL; CH471066; EAW49766.1; -; Genomic_DNA.
EMBL; CH471066; EAW49768.1; -; Genomic_DNA.
EMBL; BC003548; AAH03548.2; -; mRNA.
EMBL; BC068529; AAH68529.1; -; mRNA.
EMBL; AK022476; BAB14050.1; ALT_INIT; mRNA.
CCDS; CCDS7513.1; -. [Q9UGP5-1]
CCDS; CCDS76332.1; -. [Q9UGP5-2]
RefSeq; NP_001167555.1; NM_001174084.1. [Q9UGP5-1]
RefSeq; NP_001167556.1; NM_001174085.1.
RefSeq; NP_001295311.1; NM_001308382.1. [Q9UGP5-2]
RefSeq; NP_037406.1; NM_013274.3. [Q9UGP5-1]
RefSeq; XP_006717840.1; XM_006717777.1. [Q9UGP5-2]
RefSeq; XP_011537953.1; XM_011539651.1. [Q9UGP5-1]
UniGene; Hs.523230; -.
PDB; 1NZP; NMR; -; A=242-327.
PDB; 1RZT; X-ray; 2.10 A; A/E/I/M=245-575.
PDB; 1XSL; X-ray; 2.30 A; A/E/I/M=242-575.
PDB; 1XSN; X-ray; 1.95 A; A=242-575.
PDB; 1XSP; X-ray; 2.20 A; A=242-575.
PDB; 2BCQ; X-ray; 1.65 A; A=242-575.
PDB; 2BCR; X-ray; 1.75 A; A=242-575.
PDB; 2BCS; X-ray; 2.20 A; A=242-575.
PDB; 2BCU; X-ray; 2.20 A; A=242-575.
PDB; 2BCV; X-ray; 2.00 A; A=242-575.
PDB; 2GWS; X-ray; 2.40 A; A/E/I/M=242-575.
PDB; 2JW5; NMR; -; A=34-135.
PDB; 2PFN; X-ray; 1.90 A; A=242-575.
PDB; 2PFO; X-ray; 2.00 A; A=242-575.
PDB; 2PFP; X-ray; 2.10 A; A=242-575.
PDB; 2PFQ; X-ray; 2.10 A; A=242-575.
PDB; 3C5F; X-ray; 2.25 A; A/B=242-575.
PDB; 3C5G; X-ray; 2.20 A; A/B=242-575.
PDB; 3HW8; X-ray; 1.95 A; A=242-575.
PDB; 3HWT; X-ray; 1.95 A; A=242-575.
PDB; 3HX0; X-ray; 3.00 A; A/F/K/P=242-575.
PDB; 3MDA; X-ray; 2.03 A; A=252-575.
PDB; 3MDC; X-ray; 2.00 A; A=252-575.
PDB; 3MGH; X-ray; 2.40 A; A/C=242-462, A/C=472-575.
PDB; 3MGI; X-ray; 2.60 A; A=242-462, A=472-575.
PDB; 3PML; X-ray; 2.60 A; A/B=242-575.
PDB; 3PMN; X-ray; 2.20 A; A=242-575.
PDB; 3PNC; X-ray; 2.00 A; A=242-575.
PDB; 3UPQ; X-ray; 1.95 A; A=242-575.
PDB; 3UQ0; X-ray; 2.14 A; A=242-575.
PDB; 3UQ2; X-ray; 2.25 A; A=242-575.
PDB; 4FO6; X-ray; 2.01 A; A=242-575.
PDB; 4K4G; X-ray; 2.15 A; A/E/I/M=245-575.
PDB; 4K4H; X-ray; 2.10 A; A/E/I/M=245-575.
PDB; 4K4I; X-ray; 2.25 A; A/E/I/M=245-575.
PDB; 4X5V; X-ray; 2.15 A; A=251-575.
PDB; 4XA5; X-ray; 1.90 A; A=251-575.
PDB; 4XQ8; X-ray; 2.80 A; A/B=242-575.
PDB; 4XRH; X-ray; 3.00 A; A/B=242-575.
PDB; 4XUS; X-ray; 2.40 A; A=251-575.
PDB; 5CA7; X-ray; 2.52 A; A/B=242-575.
PDB; 5CB1; X-ray; 3.30 A; A/B=250-575.
PDB; 5CHG; X-ray; 2.90 A; A/B=242-575.
PDB; 5CJ7; X-ray; 2.90 A; A/B=242-575.
PDB; 5CP2; X-ray; 2.36 A; A/B=242-575.
PDB; 5CR0; X-ray; 2.75 A; A/B=242-575.
PDB; 5CWR; X-ray; 2.50 A; A/B=250-575.
PDB; 5DDM; X-ray; 2.80 A; A/B=242-575.
PDB; 5DDY; X-ray; 3.36 A; A/C/E/G=242-575.
PDB; 5DKW; X-ray; 2.69 A; A/B=249-575.
PDB; 5III; X-ray; 1.80 A; A=242-575.
PDB; 5IIJ; X-ray; 1.72 A; A=242-575.
PDB; 5IIK; X-ray; 1.98 A; A=242-575.
PDB; 5IIL; X-ray; 1.96 A; A=242-575.
PDB; 5IIM; X-ray; 1.94 A; A=242-575.
PDB; 5IIN; X-ray; 2.15 A; A=242-575.
PDB; 5IIO; X-ray; 2.08 A; A/E/I/M=242-575.
PDBsum; 1NZP; -.
PDBsum; 1RZT; -.
PDBsum; 1XSL; -.
PDBsum; 1XSN; -.
PDBsum; 1XSP; -.
PDBsum; 2BCQ; -.
PDBsum; 2BCR; -.
PDBsum; 2BCS; -.
PDBsum; 2BCU; -.
PDBsum; 2BCV; -.
PDBsum; 2GWS; -.
PDBsum; 2JW5; -.
PDBsum; 2PFN; -.
PDBsum; 2PFO; -.
PDBsum; 2PFP; -.
PDBsum; 2PFQ; -.
PDBsum; 3C5F; -.
PDBsum; 3C5G; -.
PDBsum; 3HW8; -.
PDBsum; 3HWT; -.
PDBsum; 3HX0; -.
PDBsum; 3MDA; -.
PDBsum; 3MDC; -.
PDBsum; 3MGH; -.
PDBsum; 3MGI; -.
PDBsum; 3PML; -.
PDBsum; 3PMN; -.
PDBsum; 3PNC; -.
PDBsum; 3UPQ; -.
PDBsum; 3UQ0; -.
PDBsum; 3UQ2; -.
PDBsum; 4FO6; -.
PDBsum; 4K4G; -.
PDBsum; 4K4H; -.
PDBsum; 4K4I; -.
PDBsum; 4X5V; -.
PDBsum; 4XA5; -.
PDBsum; 4XQ8; -.
PDBsum; 4XRH; -.
PDBsum; 4XUS; -.
PDBsum; 5CA7; -.
PDBsum; 5CB1; -.
PDBsum; 5CHG; -.
PDBsum; 5CJ7; -.
PDBsum; 5CP2; -.
PDBsum; 5CR0; -.
PDBsum; 5CWR; -.
PDBsum; 5DDM; -.
PDBsum; 5DDY; -.
PDBsum; 5DKW; -.
PDBsum; 5III; -.
PDBsum; 5IIJ; -.
PDBsum; 5IIK; -.
PDBsum; 5IIL; -.
PDBsum; 5IIM; -.
PDBsum; 5IIN; -.
PDBsum; 5IIO; -.
ProteinModelPortal; Q9UGP5; -.
SMR; Q9UGP5; -.
BioGrid; 118155; 45.
DIP; DIP-48999N; -.
IntAct; Q9UGP5; 37.
MINT; MINT-3079892; -.
STRING; 9606.ENSP00000299206; -.
BindingDB; Q9UGP5; -.
ChEMBL; CHEMBL5367; -.
iPTMnet; Q9UGP5; -.
PhosphoSitePlus; Q9UGP5; -.
BioMuta; POLL; -.
DMDM; 17367126; -.
EPD; Q9UGP5; -.
PaxDb; Q9UGP5; -.
PeptideAtlas; Q9UGP5; -.
PRIDE; Q9UGP5; -.
Ensembl; ENST00000299206; ENSP00000299206; ENSG00000166169. [Q9UGP5-1]
Ensembl; ENST00000370162; ENSP00000359181; ENSG00000166169. [Q9UGP5-1]
Ensembl; ENST00000370169; ENSP00000359188; ENSG00000166169. [Q9UGP5-1]
Ensembl; ENST00000628479; ENSP00000485885; ENSG00000166169. [Q9UGP5-2]
GeneID; 27343; -.
KEGG; hsa:27343; -.
UCSC; uc001ktg.2; human. [Q9UGP5-1]
CTD; 27343; -.
DisGeNET; 27343; -.
EuPathDB; HostDB:ENSG00000166169.16; -.
GeneCards; POLL; -.
HGNC; HGNC:9184; POLL.
HPA; HPA066704; -.
MIM; 606343; gene.
neXtProt; NX_Q9UGP5; -.
OpenTargets; ENSG00000166169; -.
PharmGKB; PA33504; -.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
GeneTree; ENSGT00530000063002; -.
HOGENOM; HOG000007787; -.
HOVERGEN; HBG002788; -.
InParanoid; Q9UGP5; -.
KO; K03512; -.
OMA; PKRKKIH; -.
OrthoDB; EOG091G03V5; -.
PhylomeDB; Q9UGP5; -.
TreeFam; TF103011; -.
BRENDA; 4.2.99.B1; 2681.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
SABIO-RK; Q9UGP5; -.
EvolutionaryTrace; Q9UGP5; -.
GeneWiki; DNA_polymerase_lambda; -.
GenomeRNAi; 27343; -.
PRO; PR:Q9UGP5; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000166169; -.
CleanEx; HS_POLL; -.
ExpressionAtlas; Q9UGP5; baseline and differential.
Genevisible; Q9UGP5; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006287; P:base-excision repair, gap-filling; IDA:UniProtKB.
GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; NAS:UniProtKB.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 1.10.150.110; -; 1.
Gene3D; 3.30.210.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR037160; DNA_Pol_thumb_sf.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR002008; DNA_pol_X_beta-like.
InterPro; IPR027421; DNA_pol_X_lyase_dom.
InterPro; IPR029398; PolB_thumb.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00870; DNAPOLXBETA.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; DNA replication; DNA synthesis; DNA-binding;
DNA-directed DNA polymerase; Lyase; Manganese; Metal-binding;
Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome;
Transferase.
CHAIN 1 575 DNA polymerase lambda.
/FTId=PRO_0000218783.
DOMAIN 36 132 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
NP_BIND 417 420 dCTP binding. {ECO:0000244|PDB:2PFP,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
NP_BIND 426 429 dCTP binding. {ECO:0000244|PDB:2PFP,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
REGION 265 279 DNA binding.
{ECO:0000269|PubMed:14992725}.
REGION 345 348 DNA binding.
{ECO:0000269|PubMed:14992725}.
REGION 420 429 Involved in primer binding.
{ECO:0000250}.
REGION 466 505 DNA binding.
{ECO:0000269|PubMed:14992725}.
ACT_SITE 312 312 Schiff-base intermediate with DNA.
{ECO:0000269|PubMed:11457865}.
METAL 427 427 Manganese. {ECO:0000244|PDB:2PFO,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
METAL 429 429 Manganese. {ECO:0000244|PDB:2PFO,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
METAL 490 490 Manganese. {ECO:0000244|PDB:2PFO,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
BINDING 386 386 dCTP. {ECO:0000244|PDB:2PFP,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
BINDING 513 513 dCTP. {ECO:0000244|PDB:2PFP,
ECO:0000244|PDB:2PFQ,
ECO:0000269|PubMed:17475573}.
VAR_SEQ 1 22 MDPRGILKAFPKRQKIHADASS -> MLMHHQKYLQRFLGG
KREKKQK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056540.
VAR_SEQ 23 297 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056541.
VARIANT 221 221 T -> P (in dbSNP:rs3730463).
/FTId=VAR_020268.
VARIANT 438 438 R -> W (changed DNA polymerase activity
characterized by decreased fidelity and
unchanged polymerization capacity;
changed function in DNA double-strand
break repair by non-homologous end
joining and homologous recombination; no
effect on 5'-deoxyribose-5-phosphate
lyase activity; dbSNP:rs3730477).
{ECO:0000269|PubMed:19806195,
ECO:0000269|PubMed:20693240,
ECO:0000269|Ref.4}.
/FTId=VAR_020269.
MUTAGEN 312 312 K->A: Reduces dRP lyase activity by over
90%. {ECO:0000269|PubMed:11457865}.
MUTAGEN 427 427 D->A: Loss of polymerase activity; when
associated with A-429.
{ECO:0000269|PubMed:19806195}.
MUTAGEN 429 429 D->A: Loss of polymerase activity; when
associated with A-427.
{ECO:0000269|PubMed:19806195}.
MUTAGEN 505 505 Y->A: No effect on polymerase activity.
Reduces terminal transferase activities.
{ECO:0000269|PubMed:14627824}.
MUTAGEN 506 506 F->G,R: Strongly reduces polymerase and
terminal transferase activities.
{ECO:0000269|PubMed:14627824}.
CONFLICT 138 138 Y -> C (in Ref. 3; AAG22519).
{ECO:0000305}.
CONFLICT 298 298 E -> G (in Ref. 7; AAH68529).
{ECO:0000305}.
HELIX 37 39 {ECO:0000244|PDB:2JW5}.
HELIX 41 43 {ECO:0000244|PDB:2JW5}.
TURN 50 52 {ECO:0000244|PDB:2JW5}.
STRAND 55 57 {ECO:0000244|PDB:2JW5}.
HELIX 60 67 {ECO:0000244|PDB:2JW5}.
STRAND 82 85 {ECO:0000244|PDB:2JW5}.
STRAND 87 89 {ECO:0000244|PDB:2JW5}.
HELIX 91 97 {ECO:0000244|PDB:2JW5}.
STRAND 108 111 {ECO:0000244|PDB:2JW5}.
HELIX 112 120 {ECO:0000244|PDB:2JW5}.
HELIX 127 129 {ECO:0000244|PDB:2JW5}.
STRAND 247 250 {ECO:0000244|PDB:1NZP}.
HELIX 254 269 {ECO:0000244|PDB:2BCQ}.
HELIX 273 287 {ECO:0000244|PDB:2BCQ}.
STRAND 289 291 {ECO:0000244|PDB:3HW8}.
HELIX 296 300 {ECO:0000244|PDB:2BCQ}.
HELIX 307 318 {ECO:0000244|PDB:2BCQ}.
STRAND 319 321 {ECO:0000244|PDB:2BCQ}.
HELIX 323 327 {ECO:0000244|PDB:2BCQ}.
HELIX 332 339 {ECO:0000244|PDB:2BCQ}.
HELIX 346 354 {ECO:0000244|PDB:2BCQ}.
HELIX 360 366 {ECO:0000244|PDB:2BCQ}.
HELIX 371 378 {ECO:0000244|PDB:2BCQ}.
TURN 379 381 {ECO:0000244|PDB:2BCQ}.
HELIX 382 384 {ECO:0000244|PDB:2BCQ}.
HELIX 389 404 {ECO:0000244|PDB:2BCQ}.
STRAND 411 414 {ECO:0000244|PDB:2BCQ}.
HELIX 416 419 {ECO:0000244|PDB:2BCQ}.
STRAND 423 433 {ECO:0000244|PDB:2BCQ}.
STRAND 435 438 {ECO:0000244|PDB:4X5V}.
TURN 439 442 {ECO:0000244|PDB:2BCQ}.
HELIX 444 453 {ECO:0000244|PDB:2BCQ}.
STRAND 457 462 {ECO:0000244|PDB:2BCQ}.
STRAND 466 468 {ECO:0000244|PDB:5IIM}.
STRAND 472 477 {ECO:0000244|PDB:2BCQ}.
STRAND 480 483 {ECO:0000244|PDB:4XA5}.
STRAND 487 493 {ECO:0000244|PDB:2BCQ}.
HELIX 496 498 {ECO:0000244|PDB:2BCQ}.
HELIX 499 507 {ECO:0000244|PDB:2BCQ}.
HELIX 510 522 {ECO:0000244|PDB:2BCQ}.
STRAND 525 527 {ECO:0000244|PDB:5IIJ}.
STRAND 532 535 {ECO:0000244|PDB:2BCQ}.
TURN 540 542 {ECO:0000244|PDB:4K4H}.
STRAND 544 546 {ECO:0000244|PDB:2BCQ}.
STRAND 549 551 {ECO:0000244|PDB:2PFN}.
HELIX 556 562 {ECO:0000244|PDB:2BCQ}.
HELIX 570 573 {ECO:0000244|PDB:2BCQ}.
SEQUENCE 575 AA; 63482 MW; FD9196A1C94923C4 CRC64;
MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR TGIGRARAEL
FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL PQLPPGAQLV KSAWLSLCLQ
ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ
KAKEAPNTQA QPISDDEASD GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV
CAQPSSQKAT NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC
SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ MWYQQGFRSL
EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ KAAQAFNSGL LCVACGSYRR
GKATCGDVDV LITHPDGRSH RGIFSRLLDS LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP
GPGRRHRRLD IIVVPYSEFA CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT
HGCKVGPGRV LPTPTEKDVF RLLGLPYREP AERDW


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