Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UGP5 (DPOLL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase lambda

Short name=Pol Lambda
EC=2.7.7.7
EC=4.2.99.-
Alternative name(s):
DNA polymerase beta-2
Short name=Pol beta2
DNA polymerase kappa
Gene names
Name:POLL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. Ref.9 Ref.13

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Manganese.

Subunit structure

Binds PCNA.

Subcellular location

Nucleus.

Tissue specificity

Expressed in a number of tissues. Abundant in testis.

Sequence similarities

Belongs to the DNA polymerase type-X family.

Contains 1 BRCT domain.

Sequence caution

The sequence BAB14050.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575DNA polymerase lambda
PRO_0000218783

Regions

Domain36 – 13297BRCT
Region265 – 27915DNA binding
Region345 – 3484DNA binding
Region420 – 42910Involved in primer binding By similarity
Region466 – 50540DNA binding

Sites

Active site3121Schiff-base intermediate with DNA
Metal binding4271Manganese By similarity
Metal binding4291Manganese By similarity
Metal binding4901Manganese By similarity

Natural variations

Natural variant2211T → P.
Corresponds to variant rs3730463 [ dbSNP | Ensembl ].
VAR_020268
Natural variant4381R → W. Ref.4
Corresponds to variant rs3730477 [ dbSNP | Ensembl ].
VAR_020269

Experimental info

Mutagenesis3121K → A: Reduces dRP lyase activity by over 90%. Ref.9
Mutagenesis5051Y → A: No effect on polymerase activity. Reduces terminal transferase activitites. Ref.11
Mutagenesis5061F → G or R: Strongly reduces polymerase and terminal transferase activitites. Ref.11
Sequence conflict1381Y → C in AAG22519. Ref.3
Sequence conflict2981E → G in AAH68529. Ref.7

Secondary structure

....................................................................................... 575
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UGP5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FD9196A1C94923C4

FASTA57563,482
        10         20         30         40         50         60 
MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR TGIGRARAEL 

        70         80         90        100        110        120 
FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL PQLPPGAQLV KSAWLSLCLQ 

       130        140        150        160        170        180 
ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ 

       190        200        210        220        230        240 
KAKEAPNTQA QPISDDEASD GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV 

       250        260        270        280        290        300 
CAQPSSQKAT NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC 

       310        320        330        340        350        360 
SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ MWYQQGFRSL 

       370        380        390        400        410        420 
EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ KAAQAFNSGL LCVACGSYRR 

       430        440        450        460        470        480 
GKATCGDVDV LITHPDGRSH RGIFSRLLDS LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP 

       490        500        510        520        530        540 
GPGRRHRRLD IIVVPYSEFA CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT 

       550        560        570 
HGCKVGPGRV LPTPTEKDVF RLLGLPYREP AERDW 

« Hide

References

« Hide 'large scale' references
[1]"DNA polymerase kappa, a new mammalian meiotic polymerase."
Garcia M., Dominguez O., Saniger M.L., Garcia M.J., Martinez C., Bernad A., Blanco L.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Two novel human and mouse DNA polymerases of the polX family."
Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S., Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.
Nucleic Acids Res. 28:3684-3693(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymph node.
[3]"Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta-related enzyme."
Nagasawa K.I., Kitamura K., Yasui A., Nimura Y., Ikeda K., Hirai M., Matsukage A., Nakanishi M.
J. Biol. Chem. 275:31233-31238(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]NIEHS SNPs program
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-438.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
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. expand/collapse author list , 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.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-575.
Tissue: Mammary gland.
[9]"Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair."
Garcia-Diaz M., Bebenek K., Kunkel T.A., Blanco L.
J. Biol. Chem. 276:34659-34663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-312.
[10]"Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study."
Blanca G., Shevelev I., Ramadan K., Villani G., Spadari S., Huebscher U., Maga G.
Biochemistry 42:7467-7476(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and Phe506 for both DNA polymerase and terminal transferase activities."
Shevelev I., Blanca G., Villani G., Ramadan K., Spadari S., Huebscher U., Maga G.
Nucleic Acids Res. 31:6916-6925(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-505 AND PHE-506.
[12]"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."
Maga G., Blanca G., Shevelev I., Frouin I., Ramadan K., Spadari S., Villani G., Huebscher U.
FASEB J. 18:1743-1745(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCNA.
[13]"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."
Maga G., Ramadan K., Locatelli G.A., Shevelev I., Spadari S., Hubscher U.
J. Biol. Chem. 280:1971-1981(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Solution structure of the lyase domain of human DNA polymerase lambda."
DeRose E.F., Kirby T.W., Mueller G.A., Bebenek K., Garcia-Diaz M., Blanco L., Kunkel T.A., London R.E.
Biochemistry 42:9564-9574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 241-327.
[15]"A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology."
Garcia-Diaz M., Bebenek K., Krahn J.M., Blanco L., Kunkel T.A., Pedersen L.C.
Mol. Cell 13:561-572(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 245-575 IN COMPLEX WITH GAPPED DNA.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131890 mRNA. Translation: CAB65074.1.
AF161019 mRNA. Translation: AAF27541.1.
AF283478 mRNA. Translation: AAG22519.1.
AF525924 Genomic DNA. Translation: AAM77696.1.
AL627424 Genomic DNA. Translation: CAI41032.1.
CH471066 Genomic DNA. Translation: EAW49759.1.
CH471066 Genomic DNA. Translation: EAW49766.1.
CH471066 Genomic DNA. Translation: EAW49768.1.
BC068529 mRNA. Translation: AAH68529.1.
AK022476 mRNA. Translation: BAB14050.1. Different initiation.
CCDSCCDS7513.1.
RefSeqNP_001167555.1. NM_001174084.1.
NP_001167556.1. NM_001174085.1.
NP_037406.1. NM_013274.3.
XP_006717833.1. XM_006717770.1.
XP_006717834.1. XM_006717771.1.
UniGeneHs.523230.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NZPNMR-A242-327[»]
1RZTX-ray2.10A/E/I/M245-575[»]
1XSLX-ray2.30A/E/I/M242-575[»]
1XSNX-ray1.95A242-575[»]
1XSPX-ray2.20A242-575[»]
2BCQX-ray1.65A242-575[»]
2BCRX-ray1.75A242-575[»]
2BCSX-ray2.20A242-575[»]
2BCUX-ray2.20A242-575[»]
2BCVX-ray2.00A242-575[»]
2GWSX-ray2.40A/E/I/M242-575[»]
2JW5NMR-A34-135[»]
2PFNX-ray1.90A242-575[»]
2PFOX-ray2.00A242-575[»]
2PFPX-ray2.10A242-575[»]
2PFQX-ray2.10A242-575[»]
3C5FX-ray2.25A/B242-575[»]
3C5GX-ray2.20A/B242-575[»]
3HW8X-ray1.95A242-575[»]
3HWTX-ray1.95A242-575[»]
3HX0X-ray3.00A/F/K/P242-575[»]
3MDAX-ray2.03A252-575[»]
3MDCX-ray2.00A252-575[»]
3MGHX-ray2.40A/C242-462[»]
A/C472-575[»]
3MGIX-ray2.60A242-462[»]
A472-575[»]
3PMLX-ray2.60A/B242-575[»]
3PMNX-ray2.20A242-575[»]
3PNCX-ray2.00A242-575[»]
3UPQX-ray1.95A242-575[»]
3UQ0X-ray2.14A242-575[»]
3UQ2X-ray2.25A242-575[»]
4FO6X-ray2.01A242-575[»]
ProteinModelPortalQ9UGP5.
SMRQ9UGP5. Positions 34-135, 252-575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118155. 9 interactions.
DIPDIP-48999N.
IntActQ9UGP5. 2 interactions.
MINTMINT-3079892.
STRING9606.ENSP00000299206.

Chemistry

BindingDBQ9UGP5.
ChEMBLCHEMBL5367.

PTM databases

PhosphoSiteQ9UGP5.

Polymorphism databases

DMDM17367126.

Proteomic databases

MaxQBQ9UGP5.
PaxDbQ9UGP5.
PRIDEQ9UGP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299206; ENSP00000299206; ENSG00000166169.
ENST00000370162; ENSP00000359181; ENSG00000166169.
ENST00000370169; ENSP00000359188; ENSG00000166169.
GeneID27343.
KEGGhsa:27343.
UCSCuc001ktg.1. human.

Organism-specific databases

CTD27343.
GeneCardsGC10M103328.
HGNCHGNC:9184. POLL.
MIM606343. gene.
neXtProtNX_Q9UGP5.
PharmGKBPA33504.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1796.
HOGENOMHOG000007787.
HOVERGENHBG002788.
InParanoidQ9UGP5.
KOK03512.
OMAWTEELIP.
OrthoDBEOG73Z2SX.
PhylomeDBQ9UGP5.
TreeFamTF103011.

Enzyme and pathway databases

SABIO-RKQ9UGP5.

Gene expression databases

ArrayExpressQ9UGP5.
BgeeQ9UGP5.
CleanExHS_POLL.
GenevestigatorQ9UGP5.

Family and domain databases

Gene3D1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR002008. DNA_pol_X_beta-like.
IPR027421. DNA_pol_X_lyase_dom.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR029398. PolB_thumb.
[Graphical view]
PfamPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PRINTSPR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTSM00278. HhH1. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF81585. SSF81585. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UGP5.
GeneWikiDNA_polymerase_lambda.
GenomeRNAi27343.
NextBio50422.
PROQ9UGP5.
SOURCESearch...

Entry information

Entry nameDPOLL_HUMAN
AccessionPrimary (citable) accession number: Q9UGP5
Secondary accession number(s): D3DR76 expand/collapse secondary AC list , Q5JQP5, Q6NUM2, Q9HA10, Q9HB35
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM