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Q9UGP5

- DPOLL_HUMAN

UniProt

Q9UGP5 - DPOLL_HUMAN

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Protein
DNA polymerase lambda
Gene
POLL
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Manganese.

Sites

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. DNA-directed DNA polymerase activity Source: UniProtKB
  3. lyase activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. DNA-dependent DNA replication Source: GOC
  3. nucleotide-excision repair Source: UniProtKB
  4. 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

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: Chromosome 10

Organism-specific databases

HGNCiHGNC:9184. POLL.

Subcellular locationi

GO - Cellular componenti

  1. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575DNA polymerase lambda
PRO_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

ArrayExpressiQ9UGP5.
BgeeiQ9UGP5.
CleanExiHS_POLL.
GenevestigatoriQ9UGP5.

Interactioni

Subunit structurei

Binds PCNA.

Protein-protein interaction databases

BioGridi118155. 9 interactions.
DIPiDIP-48999N.
IntActiQ9UGP5. 2 interactions.
MINTiMINT-3079892.
STRINGi9606.ENSP00000299206.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliQ9UGP5.
SMRiQ9UGP5. Positions 34-135, 252-575.

Miscellaneous databases

EvolutionaryTraceiQ9UGP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 13297BRCT
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 BRCT domain.

Phylogenomic databases

eggNOGiCOG1796.
HOGENOMiHOG000007787.
HOVERGENiHBG002788.
InParanoidiQ9UGP5.
KOiK03512.
OMAiWTEELIP.
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]

Sequencei

Sequence statusi: Complete.

Q9UGP5-1 [UniParc]FASTAAdd to Basket

« Hide

MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR    50
TGIGRARAEL FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL 100
PQLPPGAQLV KSAWLSLCLQ ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD 150
ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ KAKEAPNTQA QPISDDEASD 200
GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV CAQPSSQKAT 250
NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC 300
SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ 350
MWYQQGFRSL EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ 400
KAAQAFNSGL LCVACGSYRR GKATCGDVDV LITHPDGRSH RGIFSRLLDS 450
LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP GPGRRHRRLD IIVVPYSEFA 500
CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT HGCKVGPGRV 550
LPTPTEKDVF RLLGLPYREP AERDW 575
Length:575
Mass (Da):63,482
Last modified:May 1, 2000 - v1
Checksum:iFD9196A1C94923C4
GO

Sequence cautioni

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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381Y → C in AAG22519. 1 Publication
Sequence conflicti298 – 2981E → G in AAH68529. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: EAW49766.1.
CH471066 Genomic DNA. Translation: EAW49768.1.
BC068529 mRNA. Translation: AAH68529.1.
AK022476 mRNA. Translation: BAB14050.1. Different initiation.
CCDSiCCDS7513.1.
RefSeqiNP_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.
UniGeneiHs.523230.

Genome annotation databases

EnsembliENST00000299206; ENSP00000299206; ENSG00000166169.
ENST00000370162; ENSP00000359181; ENSG00000166169.
ENST00000370169; ENSP00000359188; ENSG00000166169.
GeneIDi27343.
KEGGihsa:27343.
UCSCiuc001ktg.1. human.

Polymorphism databases

DMDMi17367126.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: EAW49766.1 .
CH471066 Genomic DNA. Translation: EAW49768.1 .
BC068529 mRNA. Translation: AAH68529.1 .
AK022476 mRNA. Translation: BAB14050.1 . Different initiation.
CCDSi CCDS7513.1.
RefSeqi NP_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.
UniGenei Hs.523230.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NZP NMR - A 242-327 [» ]
1RZT X-ray 2.10 A/E/I/M 245-575 [» ]
1XSL X-ray 2.30 A/E/I/M 242-575 [» ]
1XSN X-ray 1.95 A 242-575 [» ]
1XSP X-ray 2.20 A 242-575 [» ]
2BCQ X-ray 1.65 A 242-575 [» ]
2BCR X-ray 1.75 A 242-575 [» ]
2BCS X-ray 2.20 A 242-575 [» ]
2BCU X-ray 2.20 A 242-575 [» ]
2BCV X-ray 2.00 A 242-575 [» ]
2GWS X-ray 2.40 A/E/I/M 242-575 [» ]
2JW5 NMR - A 34-135 [» ]
2PFN X-ray 1.90 A 242-575 [» ]
2PFO X-ray 2.00 A 242-575 [» ]
2PFP X-ray 2.10 A 242-575 [» ]
2PFQ X-ray 2.10 A 242-575 [» ]
3C5F X-ray 2.25 A/B 242-575 [» ]
3C5G X-ray 2.20 A/B 242-575 [» ]
3HW8 X-ray 1.95 A 242-575 [» ]
3HWT X-ray 1.95 A 242-575 [» ]
3HX0 X-ray 3.00 A/F/K/P 242-575 [» ]
3MDA X-ray 2.03 A 252-575 [» ]
3MDC X-ray 2.00 A 252-575 [» ]
3MGH X-ray 2.40 A/C 242-462 [» ]
A/C 472-575 [» ]
3MGI X-ray 2.60 A 242-462 [» ]
A 472-575 [» ]
3PML X-ray 2.60 A/B 242-575 [» ]
3PMN X-ray 2.20 A 242-575 [» ]
3PNC X-ray 2.00 A 242-575 [» ]
3UPQ X-ray 1.95 A 242-575 [» ]
3UQ0 X-ray 2.14 A 242-575 [» ]
3UQ2 X-ray 2.25 A 242-575 [» ]
4FO6 X-ray 2.01 A 242-575 [» ]
ProteinModelPortali Q9UGP5.
SMRi Q9UGP5. Positions 34-135, 252-575.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118155. 9 interactions.
DIPi DIP-48999N.
IntActi Q9UGP5. 2 interactions.
MINTi MINT-3079892.
STRINGi 9606.ENSP00000299206.

Chemistry

BindingDBi Q9UGP5.
ChEMBLi CHEMBL5367.

PTM databases

PhosphoSitei Q9UGP5.

Polymorphism databases

DMDMi 17367126.

Proteomic databases

MaxQBi Q9UGP5.
PaxDbi Q9UGP5.
PRIDEi Q9UGP5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299206 ; ENSP00000299206 ; ENSG00000166169 .
ENST00000370162 ; ENSP00000359181 ; ENSG00000166169 .
ENST00000370169 ; ENSP00000359188 ; ENSG00000166169 .
GeneIDi 27343.
KEGGi hsa:27343.
UCSCi uc001ktg.1. human.

Organism-specific databases

CTDi 27343.
GeneCardsi GC10M103328.
HGNCi HGNC:9184. POLL.
MIMi 606343. gene.
neXtProti NX_Q9UGP5.
PharmGKBi PA33504.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1796.
HOGENOMi HOG000007787.
HOVERGENi HBG002788.
InParanoidi Q9UGP5.
KOi K03512.
OMAi WTEELIP.
OrthoDBi EOG73Z2SX.
PhylomeDBi Q9UGP5.
TreeFami TF103011.

Enzyme and pathway databases

SABIO-RK Q9UGP5.

Miscellaneous databases

EvolutionaryTracei Q9UGP5.
GeneWikii DNA_polymerase_lambda.
GenomeRNAii 27343.
NextBioi 50422.
PROi Q9UGP5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UGP5.
Bgeei Q9UGP5.
CleanExi HS_POLL.
Genevestigatori Q9UGP5.

Family and domain databases

Gene3Di 1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. 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 ]
Pfami PF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view ]
PRINTSi PR00869. DNAPOLX.
PR00870. DNAPOLXBETA.
SMARTi SM00278. HhH1. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
    Tissue: Placenta.
  2. 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.
    , 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].
    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.
    , 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. 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, Q9HA10, Q9HB35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 141 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

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