POLL

Functionⁱ

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).8 Publications

Catalytic activityⁱ

a 2'-deoxyribonucleoside 5'-triphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
DNA_(n)
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Search chemical reactions in Rhea for this molecule.
=
diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
DNA_(n+1)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY.
- Ref.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), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-505 AND PHE-506.
- Ref.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, CATALYTIC ACTIVITY.
- Ref.14
  "Characterization of a natural mutator variant of human DNA polymerase lambda which promotes chromosomal instability by compromising NHEJ."
  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.
  PLoS ONE 4:E7290-E7290(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, VARIANT TRP-438, CHARACTERIZATION OF VARIANT TRP-438, MUTAGENESIS OF ASP-427 AND ASP-429.
EC:
2.7.7.7
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY.
- Ref.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), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-505 AND PHE-506.
- Ref.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, CATALYTIC ACTIVITY.
- Ref.14
  "Characterization of a natural mutator variant of human DNA polymerase lambda which promotes chromosomal instability by compromising NHEJ."
  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.
  PLoS ONE 4:E7290-E7290(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, VARIANT TRP-438, CHARACTERIZATION OF VARIANT TRP-438, MUTAGENESIS OF ASP-427 AND ASP-429.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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a 2'-deoxyribonucleoside 5'-triphosphate
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DNA_(n)
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=
diphosphate
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DNA_(n+1)
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Cofactorⁱ

Mn²⁺1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	312	Schiff-base intermediate with DNA1 Publication	1
Binding siteⁱ	386	dCTPCombined sources1 Publication	1
Metal bindingⁱ	427	ManganeseCombined sources1 Publication	1
Metal bindingⁱ	429	ManganeseCombined sources1 Publication	1
Metal bindingⁱ	490	ManganeseCombined sources1 Publication	1
Binding siteⁱ	513	dCTPCombined sources1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	417 – 420	dCTP bindingCombined sources1 Publication		4
Nucleotide bindingⁱ	426 – 429	dCTP bindingCombined sources1 Publication		4

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase
Biological process	DNA damage, DNA repair, DNA replication, DNA synthesis
Ligand	Manganese, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	4.2.99.B1, 2681
PathwayCommonsⁱ	Q9UGP5
Reactomeⁱ	R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
SABIO-RKⁱ	Q9UGP5

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA polymerase lambdaCurated (EC:2.7.7.76 Publications, EC:4.2.99.-2 Publications) Short name: Pol LambdaCurated Alternative name(s): DNA polymerase beta-21 Publication Short name: Pol beta21 Publication DNA polymerase kappa1 Publication
Gene namesⁱ	Name:POLLImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000166169.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9184, POLL
MIMⁱ	606343, gene
neXtProtⁱ	NX_Q9UGP5

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	312	K → A: Reduces dRP lyase activity by over 90%. 1 Publication	1
Mutagenesisⁱ	427	D → A: Loss of polymerase activity; when associated with A-429. 1 Publication	1
Mutagenesisⁱ	429	D → A: Loss of polymerase activity; when associated with A-427. 1 Publication	1
Mutagenesisⁱ	505	Y → A: No effect on polymerase activity. Reduces terminal transferase activities. 1 Publication	1
Mutagenesisⁱ	506	F → G or R: Strongly reduces polymerase and terminal transferase activities. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	27343
Open Targets More...OpenTargetsⁱ	ENSG00000166169
PharmGKBⁱ	PA33504

Miscellaneous databases

Pharosⁱ	Q9UGP5, Tbio

Pharosⁱ

Q9UGP5, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL5367

ChEMBLⁱ

CHEMBL5367

Polymorphism and mutation databases

BioMutaⁱ	POLL
DMDMⁱ	17367126

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000218783	1 – 575	DNA polymerase lambdaAdd BLAST		575

Proteomic databases

EPDⁱ	Q9UGP5
jPOSTⁱ	Q9UGP5
MassIVEⁱ	Q9UGP5
PaxDbⁱ	Q9UGP5
PeptideAtlas More...PeptideAtlasⁱ	Q9UGP5
PRIDEⁱ	Q9UGP5
ProteomicsDBⁱ	79002 84253 [Q9UGP5-1]

PTM databases

iPTMnetⁱ	Q9UGP5
PhosphoSitePlusⁱ	Q9UGP5

Expressionⁱ

Tissue specificityⁱ

Expressed in a number of tissues. Abundant in testis.

Gene expression databases

Bgeeⁱ	ENSG00000166169, Expressed in body of pancreas and 212 other tissues
ExpressionAtlasⁱ	Q9UGP5, baseline and differential
Genevisibleⁱ	Q9UGP5, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000166169, Low tissue specificity

HPAⁱ

ENSG00000166169, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Binds PCNA.

1 Publication

Binary interactionsⁱ

Hide details

Isoform 2 [Q9UGP5-2]

With	#Exp.	IntAct
CCNDBP1 [O95273]	3	EBI-10320765,EBI-748961
CMTM5 - isoform 2 [Q96DZ9-2]	3	EBI-10320765,EBI-11522780
FAM9B [Q8IZU0]	3	EBI-10320765,EBI-10175124
FSD2 [A1L4K1]	4	EBI-10320765,EBI-5661036
GOLGA6L9 [A6NEM1]	3	EBI-10320765,EBI-5916454
HMBOX1 [Q6NT76]	3	EBI-10320765,EBI-2549423
KRT16 [P08779]	3	EBI-10320765,EBI-356410
KRT19 [P08727]	3	EBI-10320765,EBI-742756
KRT27 [Q7Z3Y8]	3	EBI-10320765,EBI-3044087
KRT40 [Q6A162]	3	EBI-10320765,EBI-10171697
KRTAP10-7 [P60409]	3	EBI-10320765,EBI-10172290
LCN2 [P80188]	3	EBI-10320765,EBI-11911016
MAGEA12 [P43365]	6	EBI-10320765,EBI-749530
MAGEA2B [P43356]	3	EBI-10320765,EBI-5650739
MAL2 [Q969L2]	3	EBI-10320765,EBI-944295
MCC [P23508]	3	EBI-10320765,EBI-307531
MDFI [Q99750]	3	EBI-10320765,EBI-724076
PICK1 [Q9NRD5]	3	EBI-10320765,EBI-79165
PNMA1 [Q8ND90]	3	EBI-10320765,EBI-302345
PRKD3 - isoform 2 [O94806-2]	3	EBI-10320765,EBI-13337369
SSX2IP [Q9Y2D8]	3	EBI-10320765,EBI-2212028
TFCP2 [Q12800]	3	EBI-10320765,EBI-717422
TFIP11 [Q9UBB9]	3	EBI-10320765,EBI-1105213
TNFRSF10D [Q9UBN6]	3	EBI-10320765,EBI-1044859
TRIM23 [P36406]	3	EBI-10320765,EBI-740098
ZRANB1 [Q9UGI0]	3	EBI-10320765,EBI-527853

Protein-protein interaction databases

BioGRIDⁱ	118155, 62 interactors
Database of interacting proteins More...DIPⁱ	DIP-48999N
IntActⁱ	Q9UGP5, 41 interactors
Molecular INTeraction database More...MINTⁱ	Q9UGP5
STRINGⁱ	9606.ENSP00000359181

Chemistry databases

BindingDBⁱ

Q9UGP5

Miscellaneous databases

RNActⁱ	Q9UGP5, protein

RNActⁱ

Q9UGP5, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	37 – 39	Combined sources	3
Helixⁱ	41 – 43	Combined sources	3
Turnⁱ	50 – 52	Combined sources	3
Beta strandⁱ	55 – 57	Combined sources	3
Helixⁱ	60 – 67	Combined sources	8
Beta strandⁱ	82 – 85	Combined sources	4
Beta strandⁱ	87 – 89	Combined sources	3
Helixⁱ	91 – 97	Combined sources	7
Beta strandⁱ	108 – 111	Combined sources	4
Helixⁱ	112 – 120	Combined sources	9
Helixⁱ	127 – 129	Combined sources	3
Beta strandⁱ	247 – 250	Combined sources	4
Helixⁱ	254 – 269	Combined sources	16
Helixⁱ	273 – 287	Combined sources	15
Beta strandⁱ	289 – 291	Combined sources	3
Helixⁱ	296 – 300	Combined sources	5
Helixⁱ	307 – 318	Combined sources	12
Beta strandⁱ	319 – 321	Combined sources	3
Helixⁱ	323 – 327	Combined sources	5
Helixⁱ	332 – 339	Combined sources	8
Helixⁱ	346 – 354	Combined sources	9
Helixⁱ	360 – 366	Combined sources	7
Helixⁱ	371 – 378	Combined sources	8
Turnⁱ	379 – 381	Combined sources	3
Helixⁱ	382 – 384	Combined sources	3
Helixⁱ	389 – 404	Combined sources	16
Beta strandⁱ	411 – 414	Combined sources	4
Helixⁱ	416 – 419	Combined sources	4
Beta strandⁱ	423 – 433	Combined sources	11
Beta strandⁱ	435 – 438	Combined sources	4
Turnⁱ	439 – 442	Combined sources	4
Helixⁱ	444 – 453	Combined sources	10
Beta strandⁱ	457 – 462	Combined sources	6
Beta strandⁱ	466 – 468	Combined sources	3
Beta strandⁱ	472 – 477	Combined sources	6
Beta strandⁱ	480 – 483	Combined sources	4
Beta strandⁱ	487 – 493	Combined sources	7
Helixⁱ	496 – 498	Combined sources	3
Helixⁱ	499 – 507	Combined sources	9
Helixⁱ	510 – 522	Combined sources	13
Beta strandⁱ	525 – 527	Combined sources	3
Beta strandⁱ	532 – 535	Combined sources	4
Turnⁱ	540 – 542	Combined sources	3
Beta strandⁱ	544 – 546	Combined sources	3
Beta strandⁱ	549 – 551	Combined sources	3
Helixⁱ	556 – 562	Combined sources	7
Helixⁱ	570 – 573	Combined sources	4

Show more details

3D structure databases

BMRBⁱ	Q9UGP5
SMRⁱ	Q9UGP5
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9UGP5

EvolutionaryTraceⁱ

Q9UGP5

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	36 – 132	BRCTPROSITE-ProRule annotationAdd BLAST		97

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	265 – 279	DNA binding1 PublicationAdd BLAST	15
Regionⁱ	345 – 348	DNA binding1 Publication	4
Regionⁱ	420 – 429	Involved in primer bindingBy similarity	10
Regionⁱ	466 – 505	DNA binding1 PublicationAdd BLAST	40

Sequence similaritiesⁱ

Belongs to the DNA polymerase type-X family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2534, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158515
InParanoidⁱ	Q9UGP5
OMAⁱ	VKTAQMW
Database of Orthologous Groups More...OrthoDBⁱ	1328151at2759
PhylomeDBⁱ	Q9UGP5
TreeFamⁱ	TF103011

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00141, NT_POLXc, 1 hit
Gene3Dⁱ	1.10.150.110, 1 hit 3.30.210.10, 1 hit 3.30.460.10, 1 hit 3.40.50.10190, 1 hit
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf 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 IPR027421, DNA_pol_lamdba_lyase_dom_sf IPR037160, DNA_Pol_thumb_sf IPR022312, DNA_pol_X IPR002008, DNA_pol_X_beta-like IPR043519, NT_sf IPR029398, PolB_thumb
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF14792, DNA_pol_B_palm, 1 hit PF14791, DNA_pol_B_thumb, 1 hit PF10391, DNA_pol_lambd_f, 1 hit PF14716, HHH_8, 1 hit
PRINTSⁱ	PR00869, DNAPOLX PR00870, DNAPOLXBETA
SMARTⁱ	View protein in SMART SM00483, POLXc, 1 hit
SUPFAMⁱ	SSF47802, SSF47802, 1 hit SSF52113, SSF52113, 1 hit SSF81301, SSF81301, 1 hit
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 1 hit PS00522, DNA_POLYMERASE_X, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 2 described isoforms and 9 potential isoforms that are computationally mapped.Show all Align All

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

This isoform has been chosen as the canonicalⁱ 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MLMHHQKYLQ RFLGGKREKK QKEACSIPGI GKRMAEKIIE ILESGHLRKL 
        60         70         80         90        100
DHISESVPVL ELFSNIWGAG TKTAQMWYQQ GFRSLEDIRS QASLTTQQAI 
       110        120        130        140        150
GLKHYSDFLE RMPREEATEI EQTVQKAAQA FNSGLLCVAC GSYRRGKATC 
       160        170        180        190        200
GDVDVLITHP DGRSHRGIFS RLLDSLRQEG FLTDDLVSQE ENGQQQKYLG 
       210        220        230        240        250
VCRLPGPGRR HRRLDIIVVP YSEFACALLY FTGSAHFNRS MRALAKTKGM 
       260        270        280        290        300
SLSEHALSTA VVRNTHGCKV GPGRVLPTPT EKDVFRLLGL PYREPAERDW

Show »

Length:300

Mass (Da):33,839

Checksum:ⁱB67B993D5EC4A47C

GO

Computationally mapped potential isoform sequencesⁱ

There are 9 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q5JQP2	Q5JQP2_HUMAN	DNA polymerase DNA polymerase, EC 2.7.7.7	POLL	470	Annotation score:
Q5JQP8	Q5JQP8_HUMAN	DNA polymerase DNA polymerase, EC 2.7.7.7	POLL hCG_23002	487	Annotation score:
Q9HBN3	Q9HBN3_HUMAN	DNA polymerase DNA polymerase, EC 2.7.7.7	POLL hCG_23002	248	Annotation score:
Q5JQP3	Q5JQP3_HUMAN	DNA polymerase DNA polymerase, EC 2.7.7.7	POLL	218	Annotation score:
Q5JQP4	Q5JQP4_HUMAN	DNA polymerase DNA polymerase, EC 2.7.7.7	POLL	298	Annotation score:
Q5JQN9	Q5JQN9_HUMAN	DNA polymerase lambda DNA polymerase lambda	POLL	334	Annotation score:
Q5JQP0	Q5JQP0_HUMAN	DNA polymerase lambda DNA polymerase lambda	POLL	188	Annotation score:
Q5JQP1	Q5JQP1_HUMAN	DNA polymerase lambda DNA polymerase lambda	POLL	268	Annotation score:
Q5JQP7	Q5JQP7_HUMAN	DNA polymerase lambda DNA polymerase lambda	POLL	151	Annotation score:

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	138	Y → C in AAG22519 (PubMed:10887191).Curated		1
Sequence conflictⁱ	298	E → G in AAH68529 (PubMed:15489334).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_020268	221	T → P. Corresponds to variant dbSNP:rs3730463Ensembl.		1
Natural variantⁱVAR_020269	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. 3 PublicationsCorresponds to variant dbSNP:rs3730477Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056540	1 – 22	MDPRG…ADASS → MLMHHQKYLQRFLGGKREKK QK in isoform 2. 1 PublicationAdd BLAST		22
Alternative sequenceⁱVSP_056541	23 – 297	Missing in isoform 2. 1 PublicationAdd BLAST		275

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 No translation available. 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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7513.1 [Q9UGP5-1] CCDS76332.1 [Q9UGP5-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001167555.1, NM_001174084.1 [Q9UGP5-1] NP_001167556.1, NM_001174085.1 NP_001295311.1, NM_001308382.1 [Q9UGP5-2] NP_037406.1, NM_013274.3 [Q9UGP5-1] XP_006717840.1, XM_006717777.1 [Q9UGP5-2] XP_011537953.1, XM_011539651.1 [Q9UGP5-1]

Genome annotation databases

Ensemblⁱ	ENST00000299206; ENSP00000299206; ENSG00000166169 [Q9UGP5-1] ENST00000370162; ENSP00000359181; ENSG00000166169 [Q9UGP5-1] ENST00000370169; ENSP00000359188; ENSG00000166169 [Q9UGP5-1] ENST00000628479; ENSP00000485885; ENSG00000166169 [Q9UGP5-2]
GeneIDⁱ	27343
KEGGⁱ	hsa:27343
UCSC genome browser More...UCSCⁱ	uc001ktg.2, human [Q9UGP5-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UGP5	DNA polymerase		HUMAN		267	UniRef100_Q9UGP5
DNA polymerase (Fragment)		HUMAN		167
DNA polymerase		HUMAN		487
+5
Q9UGP5-2	DNA polymerase		HUMAN		298	UniRef100_Q5JQP4
DNA polymerase (Fragment)		HUMAN		218

Protein	Similar proteins		Species	Score	Length	Source
Q9UGP5	DNA polymerase lambda		MACFA		575	UniRef90_Q9UGP5
DNA polymerase		HUMAN		267
DNA polymerase		CALJA		639
DNA polymerase		MACMU		575
DNA polymerase		CHLSB		575
+56
Q9UGP5-2	DNA polymerase		HUMAN		298	UniRef90_Q5JQP4
DNA polymerase		PANTR		300
DNA polymerase		RHIRO		300
DNA polymerase		RHIBE		300
DNA polymerase		GORGO		300
+20

Protein	Similar proteins		Species	Score	Length	Source
Q9UGP5	DNA polymerase lambda		MACFA		575	UniRef50_Q9UGP5
DNA polymerase		HUMAN		267
DNA polymerase		CALJA		639
DNA polymerase (Fragment)		COLGU		575
DNA polymerase		COLAP		575
+215
Q9UGP5-2	DNA polymerase		PIG		300	UniRef50_A0A5G2QUL9
DNA polymerase		BOBOX		300
DNA polymerase		AMAAE		330
DNA polymerase		PROCO		300
DNA polymerase		HUMAN		267
+46

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 No translation available. 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.
CCDSⁱ	CCDS7513.1 [Q9UGP5-1] CCDS76332.1 [Q9UGP5-2]
RefSeqⁱ	NP_001167555.1, NM_001174084.1 [Q9UGP5-1] NP_001167556.1, NM_001174085.1 NP_001295311.1, NM_001308382.1 [Q9UGP5-2] NP_037406.1, NM_013274.3 [Q9UGP5-1] XP_006717840.1, XM_006717777.1 [Q9UGP5-2] XP_011537953.1, XM_011539651.1 [Q9UGP5-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	242-575	[»]
	3MGI	X-ray	2.60	A	242-575	[»]
	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	[»]
	4K4G	X-ray	2.15	A/E/I/M	245-575	[»]
	4K4H	X-ray	2.10	A/E/I/M	245-575	[»]
	4K4I	X-ray	2.25	A/E/I/M	245-575	[»]
	4X5V	X-ray	2.15	A	251-575	[»]
	4XA5	X-ray	1.90	A	251-575	[»]
	4XQ8	X-ray	2.80	A/B	242-575	[»]
	4XRH	X-ray	3.00	A/B	242-575	[»]
	4XUS	X-ray	2.40	A	251-575	[»]
	5CA7	X-ray	2.52	A/B	242-575	[»]
	5CB1	X-ray	3.30	A/B	250-575	[»]
	5CHG	X-ray	2.90	A/B	242-575	[»]
	5CJ7	X-ray	2.90	A/B	242-575	[»]
	5CP2	X-ray	2.36	A/B	242-575	[»]
	5CR0	X-ray	2.75	A/B	242-575	[»]
	5CWR	X-ray	2.50	A/B	250-575	[»]
	5DDM	X-ray	2.80	A/B	242-575	[»]
	5DDY	X-ray	3.36	A/C/E/G	242-575	[»]
	5DKW	X-ray	2.69	A/B	249-575	[»]
	5III	X-ray	1.80	A	242-575	[»]
	5IIJ	X-ray	1.72	A	242-575	[»]
	5IIK	X-ray	1.98	A	242-575	[»]
	5IIL	X-ray	1.96	A	242-575	[»]
	5IIM	X-ray	1.94	A	242-575	[»]
	5IIN	X-ray	2.15	A	242-575	[»]
	5IIO	X-ray	2.08	A/E/I/M	242-575	[»]
	5W4G	X-ray	2.04	A	4-32	[»]
BMRBⁱ	Q9UGP5
SMRⁱ	Q9UGP5
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	118155, 62 interactors
DIPⁱ	DIP-48999N
IntActⁱ	Q9UGP5, 41 interactors
MINTⁱ	Q9UGP5
STRINGⁱ	9606.ENSP00000359181

Chemistry databases

BindingDBⁱ	Q9UGP5
ChEMBLⁱ	CHEMBL5367

PTM databases

iPTMnetⁱ	Q9UGP5
PhosphoSitePlusⁱ	Q9UGP5

Polymorphism and mutation databases

BioMutaⁱ	POLL
DMDMⁱ	17367126

Proteomic databases

EPDⁱ	Q9UGP5
jPOSTⁱ	Q9UGP5
MassIVEⁱ	Q9UGP5
PaxDbⁱ	Q9UGP5
PeptideAtlasⁱ	Q9UGP5
PRIDEⁱ	Q9UGP5
ProteomicsDBⁱ	79002 84253 [Q9UGP5-1]

Protocols and materials databases

Antibodypediaⁱ	31295, 229 antibodies

Antibodypediaⁱ

31295, 229 antibodies

Genome annotation databases

Ensemblⁱ	ENST00000299206; ENSP00000299206; ENSG00000166169 [Q9UGP5-1] ENST00000370162; ENSP00000359181; ENSG00000166169 [Q9UGP5-1] ENST00000370169; ENSP00000359188; ENSG00000166169 [Q9UGP5-1] ENST00000628479; ENSP00000485885; ENSG00000166169 [Q9UGP5-2]
GeneIDⁱ	27343
KEGGⁱ	hsa:27343
UCSCⁱ	uc001ktg.2, human [Q9UGP5-1]

Organism-specific databases

CTDⁱ	27343
DisGeNETⁱ	27343
EuPathDBⁱ	HostDB:ENSG00000166169.16
GeneCardsⁱ	POLL
HGNCⁱ	HGNC:9184, POLL
HPAⁱ	ENSG00000166169, Low tissue specificity
MIMⁱ	606343, gene
neXtProtⁱ	NX_Q9UGP5
OpenTargetsⁱ	ENSG00000166169
PharmGKBⁱ	PA33504
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2534, Eukaryota
GeneTreeⁱ	ENSGT00940000158515
InParanoidⁱ	Q9UGP5
OMAⁱ	VKTAQMW
OrthoDBⁱ	1328151at2759
PhylomeDBⁱ	Q9UGP5
TreeFamⁱ	TF103011

Enzyme and pathway databases

BRENDAⁱ	4.2.99.B1, 2681
PathwayCommonsⁱ	Q9UGP5
Reactomeⁱ	R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
SABIO-RKⁱ	Q9UGP5

Miscellaneous databases

BioGRID-ORCSⁱ	27343, 3 hits in 847 CRISPR screens
ChiTaRSⁱ	POLL, human
EvolutionaryTraceⁱ	Q9UGP5
GeneWikiⁱ	DNA_polymerase_lambda
GenomeRNAiⁱ	27343
Pharosⁱ	Q9UGP5, Tbio
Protein Ontology More...PROⁱ	PR:Q9UGP5
RNActⁱ	Q9UGP5, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000166169, Expressed in body of pancreas and 212 other tissues
ExpressionAtlasⁱ	Q9UGP5, baseline and differential
Genevisibleⁱ	Q9UGP5, HS

Family and domain databases

CDDⁱ	cd00141, NT_POLXc, 1 hit
Gene3Dⁱ	1.10.150.110, 1 hit 3.30.210.10, 1 hit 3.30.460.10, 1 hit 3.40.50.10190, 1 hit
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf 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 IPR027421, DNA_pol_lamdba_lyase_dom_sf IPR037160, DNA_Pol_thumb_sf IPR022312, DNA_pol_X IPR002008, DNA_pol_X_beta-like IPR043519, NT_sf IPR029398, PolB_thumb
Pfamⁱ	View protein in Pfam PF14792, DNA_pol_B_palm, 1 hit PF14791, DNA_pol_B_thumb, 1 hit PF10391, DNA_pol_lambd_f, 1 hit PF14716, HHH_8, 1 hit
PRINTSⁱ	PR00869, DNAPOLX PR00870, DNAPOLXBETA
SMARTⁱ	View protein in SMART SM00483, POLXc, 1 hit
SUPFAMⁱ	SSF47802, SSF47802, 1 hit SSF52113, SSF52113, 1 hit SSF81301, SSF81301, 1 hit
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 1 hit PS00522, DNA_POLYMERASE_X, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DPOLL_HUMAN
Accessionⁱ	Q9UGP5Primary (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:	December 2, 2020
	This is version 199 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Reference proteome

Documents

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

UniProtKB

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UniProtKB - Q9UGP5 (DPOLL_HUMAN)

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DNA polymerase lambda

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

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Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Isoform 2 [Q9UGP5-2]

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

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<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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Sequence databases

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Chemistry databases

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Proteomic databases

Protocols and materials databases

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Organism-specific databases

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Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ