Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase lambda

Gene

POLL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei312 – 3121Schiff-base intermediate with DNA
Metal bindingi427 – 4271ManganeseBy similarity
Metal bindingi429 – 4291ManganeseBy similarity
Metal bindingi490 – 4901ManganeseBy similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • lyase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • DNA replication Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • somatic hypermutation of immunoglobulin genes Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, DNA synthesis

Keywords - Ligandi

DNA-binding, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.99.B1. 2681.
SABIO-RKQ9UGP5.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase lambda (EC:2.7.7.7, EC:4.2.99.-)
Short name:
Pol Lambda
Alternative name(s):
DNA polymerase beta-2
Short name:
Pol beta2
DNA polymerase kappa
Gene namesi
Name:POLL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9184. POLL.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi312 – 3121K → A: Reduces dRP lyase activity by over 90%. 1 Publication
Mutagenesisi505 – 5051Y → A: No effect on polymerase activity. Reduces terminal transferase activitites. 1 Publication
Mutagenesisi506 – 5061F → G or R: Strongly reduces polymerase and terminal transferase activitites. 1 Publication

Organism-specific databases

PharmGKBiPA33504.

Polymorphism and mutation databases

BioMutaiPOLL.
DMDMi17367126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575DNA polymerase lambdaPRO_0000218783Add
BLAST

Proteomic databases

MaxQBiQ9UGP5.
PaxDbiQ9UGP5.
PRIDEiQ9UGP5.

PTM databases

PhosphoSiteiQ9UGP5.

Expressioni

Tissue specificityi

Expressed in a number of tissues. Abundant in testis.

Gene expression databases

BgeeiQ9UGP5.
CleanExiHS_POLL.
ExpressionAtlasiQ9UGP5. baseline and differential.
GenevisibleiQ9UGP5. HS.

Interactioni

Subunit structurei

Binds PCNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-10320765,EBI-10175124
FSD2A1L4K14EBI-10320765,EBI-5661036
KRT40Q6A1623EBI-10320765,EBI-10171697
KRTAP10-7P604093EBI-10320765,EBI-10172290
MAGEA12Q6FHH83EBI-10320765,EBI-10178394
PNMA1Q8ND903EBI-10320765,EBI-302345
SSX2IPQ9Y2D83EBI-10320765,EBI-2212028
TFCP2Q128003EBI-10320765,EBI-717422
TFIP11Q9UBB93EBI-10320765,EBI-1105213
TRIM23P364063EBI-10320765,EBI-740098

Protein-protein interaction databases

BioGridi118155. 32 interactions.
DIPiDIP-48999N.
IntActiQ9UGP5. 13 interactions.
MINTiMINT-3079892.
STRINGi9606.ENSP00000299206.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393Combined sources
Helixi41 – 433Combined sources
Turni50 – 523Combined sources
Beta strandi55 – 573Combined sources
Helixi60 – 678Combined sources
Beta strandi82 – 854Combined sources
Beta strandi87 – 893Combined sources
Helixi91 – 977Combined sources
Beta strandi108 – 1114Combined sources
Helixi112 – 1209Combined sources
Helixi127 – 1293Combined sources
Beta strandi247 – 2504Combined sources
Helixi254 – 26916Combined sources
Helixi273 – 28715Combined sources
Beta strandi289 – 2913Combined sources
Helixi296 – 3005Combined sources
Helixi307 – 31812Combined sources
Beta strandi319 – 3213Combined sources
Helixi323 – 3275Combined sources
Helixi332 – 3398Combined sources
Helixi346 – 3549Combined sources
Helixi360 – 3667Combined sources
Helixi371 – 3788Combined sources
Turni379 – 3813Combined sources
Helixi382 – 3843Combined sources
Helixi389 – 40416Combined sources
Beta strandi411 – 4144Combined sources
Helixi416 – 4194Combined sources
Beta strandi423 – 43311Combined sources
Beta strandi435 – 4384Combined sources
Turni439 – 4424Combined sources
Helixi444 – 45310Combined sources
Beta strandi457 – 4626Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi472 – 4776Combined sources
Beta strandi480 – 4834Combined sources
Beta strandi487 – 4937Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 5079Combined sources
Helixi510 – 52213Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi532 – 5354Combined sources
Turni540 – 5423Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi549 – 5513Combined sources
Helixi556 – 5627Combined sources
Helixi570 – 5734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4K4GX-ray2.15A/E/I/M245-575[»]
4K4HX-ray2.10A/E/I/M245-575[»]
4K4IX-ray2.25A/E/I/M245-575[»]
ProteinModelPortaliQ9UGP5.
SMRiQ9UGP5. Positions 34-135, 252-575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UGP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 13297BRCTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 27915DNA bindingAdd
BLAST
Regioni345 – 3484DNA binding
Regioni420 – 42910Involved in primer bindingBy similarity
Regioni466 – 50540DNA bindingAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000007787.
HOVERGENiHBG002788.
InParanoidiQ9UGP5.
KOiK03512.
OMAiIVVDEGM.
OrthoDBiEOG73Z2SX.
PhylomeDBiQ9UGP5.
TreeFamiTF103011.

Family and domain databases

Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. 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]
PfamiPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PRINTSiPR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTiSM00278. HhH1. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UGP5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR
60 70 80 90 100
TGIGRARAEL FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL
110 120 130 140 150
PQLPPGAQLV KSAWLSLCLQ ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD
160 170 180 190 200
ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ KAKEAPNTQA QPISDDEASD
210 220 230 240 250
GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV CAQPSSQKAT
260 270 280 290 300
NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC
310 320 330 340 350
SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ
360 370 380 390 400
MWYQQGFRSL EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ
410 420 430 440 450
KAAQAFNSGL LCVACGSYRR GKATCGDVDV LITHPDGRSH RGIFSRLLDS
460 470 480 490 500
LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP GPGRRHRRLD IIVVPYSEFA
510 520 530 540 550
CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT HGCKVGPGRV
560 570
LPTPTEKDVF RLLGLPYREP AERDW
Length:575
Mass (Da):63,482
Last modified:May 1, 2000 - v1
Checksum:iFD9196A1C94923C4
GO
Isoform 2 (identifier: Q9UGP5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MDPRGILKAFPKRQKIHADASS → MLMHHQKYLQRFLGGKREKKQK
     23-297: Missing.

Note: No experimental confirmation available.
Show »
Length:300
Mass (Da):33,839
Checksum:iB67B993D5EC4A47C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381Y → C in AAG22519 (PubMed:10887191).Curated
Sequence conflicti298 – 2981E → G in AAH68529 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211T → P.
Corresponds to variant rs3730463 [ dbSNP | Ensembl ].
VAR_020268
Natural varianti438 – 4381R → W.1 Publication
Corresponds to variant rs3730477 [ dbSNP | Ensembl ].
VAR_020269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222MDPRG…ADASS → MLMHHQKYLQRFLGGKREKK QK in isoform 2. 1 PublicationVSP_056540Add
BLAST
Alternative sequencei23 – 297275Missing in isoform 2. 1 PublicationVSP_056541Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAW49760.1.
CH471066 Genomic DNA. Translation: EAW49766.1.
CH471066 Genomic DNA. Translation: EAW49768.1.
BC003548 mRNA. Translation: AAH03548.2.
BC068529 mRNA. Translation: AAH68529.1.
AK022476 mRNA. Translation: BAB14050.1. Different initiation.
CCDSiCCDS7513.1. [Q9UGP5-1]
RefSeqiNP_001167555.1. NM_001174084.1. [Q9UGP5-1]
NP_001167556.1. NM_001174085.1.
NP_037406.1. NM_013274.3. [Q9UGP5-1]
XP_006717840.1. XM_006717777.1. [Q9UGP5-2]
XP_006717841.1. XM_006717778.2. [Q9UGP5-2]
UniGeneiHs.523230.

Genome annotation databases

EnsembliENST00000299206; ENSP00000299206; ENSG00000166169. [Q9UGP5-1]
ENST00000370162; ENSP00000359181; ENSG00000166169. [Q9UGP5-1]
ENST00000370169; ENSP00000359188; ENSG00000166169. [Q9UGP5-1]
ENST00000628479; ENSP00000485885; ENSG00000166169. [Q9UGP5-2]
GeneIDi27343.
KEGGihsa:27343.
UCSCiuc001ktg.1. human. [Q9UGP5-1]
uc001kth.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAW49760.1.
CH471066 Genomic DNA. Translation: EAW49766.1.
CH471066 Genomic DNA. Translation: EAW49768.1.
BC003548 mRNA. Translation: AAH03548.2.
BC068529 mRNA. Translation: AAH68529.1.
AK022476 mRNA. Translation: BAB14050.1. Different initiation.
CCDSiCCDS7513.1. [Q9UGP5-1]
RefSeqiNP_001167555.1. NM_001174084.1. [Q9UGP5-1]
NP_001167556.1. NM_001174085.1.
NP_037406.1. NM_013274.3. [Q9UGP5-1]
XP_006717840.1. XM_006717777.1. [Q9UGP5-2]
XP_006717841.1. XM_006717778.2. [Q9UGP5-2]
UniGeneiHs.523230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4K4GX-ray2.15A/E/I/M245-575[»]
4K4HX-ray2.10A/E/I/M245-575[»]
4K4IX-ray2.25A/E/I/M245-575[»]
ProteinModelPortaliQ9UGP5.
SMRiQ9UGP5. Positions 34-135, 252-575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118155. 32 interactions.
DIPiDIP-48999N.
IntActiQ9UGP5. 13 interactions.
MINTiMINT-3079892.
STRINGi9606.ENSP00000299206.

Chemistry

BindingDBiQ9UGP5.
ChEMBLiCHEMBL5367.

PTM databases

PhosphoSiteiQ9UGP5.

Polymorphism and mutation databases

BioMutaiPOLL.
DMDMi17367126.

Proteomic databases

MaxQBiQ9UGP5.
PaxDbiQ9UGP5.
PRIDEiQ9UGP5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299206; ENSP00000299206; ENSG00000166169. [Q9UGP5-1]
ENST00000370162; ENSP00000359181; ENSG00000166169. [Q9UGP5-1]
ENST00000370169; ENSP00000359188; ENSG00000166169. [Q9UGP5-1]
ENST00000628479; ENSP00000485885; ENSG00000166169. [Q9UGP5-2]
GeneIDi27343.
KEGGihsa:27343.
UCSCiuc001ktg.1. human. [Q9UGP5-1]
uc001kth.1. human.

Organism-specific databases

CTDi27343.
GeneCardsiGC10M103328.
HGNCiHGNC:9184. POLL.
MIMi606343. gene.
neXtProtiNX_Q9UGP5.
PharmGKBiPA33504.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000007787.
HOVERGENiHBG002788.
InParanoidiQ9UGP5.
KOiK03512.
OMAiIVVDEGM.
OrthoDBiEOG73Z2SX.
PhylomeDBiQ9UGP5.
TreeFamiTF103011.

Enzyme and pathway databases

BRENDAi4.2.99.B1. 2681.
SABIO-RKQ9UGP5.

Miscellaneous databases

EvolutionaryTraceiQ9UGP5.
GeneWikiiDNA_polymerase_lambda.
GenomeRNAii27343.
NextBioi13648274.
PROiQ9UGP5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGP5.
CleanExiHS_POLL.
ExpressionAtlasiQ9UGP5. baseline and differential.
GenevisibleiQ9UGP5. HS.

Family and domain databases

Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. 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]
PfamiPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PRINTSiPR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTiSM00278. HhH1. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
  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.
    , 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. 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] (ISOFORMS 1 AND 2).
    Tissue: Lung and 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.
    , 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 (ISOFORM 1).
    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. 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.

Entry informationi

Entry nameiDPOLL_HUMAN
AccessioniPrimary (citable) accession number: Q9UGP5
Secondary accession number(s): D3DR76
, Q5JQP5, Q6NUM2, Q9BTN8, Q9HA10, Q9HB35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.