Q9UGP5 (DPOLL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR.
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.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication DNA synthesis
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding Manganese Metal-binding
Molecular function	DNA-directed DNA polymerase Lyase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Non-traceable author statement Ref.2. Source: UniProtKB nucleotide-excision repair Inferred from direct assay Ref.2. Source: UniProtKB somatic hypermutation of immunoglobulin genes Non-traceable author statement Ref.2. Source: UniProtKB
Cellular_component	nucleus Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	DNA binding Non-traceable author statement Ref.2. Source: UniProtKB DNA-directed DNA polymerase activity Non-traceable author statement Ref.2. Source: UniProtKB lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 575

575

DNA polymerase lambda

PRO_0000218783

Regions

Domain

36 – 132

97

BRCT

Region

265 – 279

15

DNA binding

Region

345 – 348

4

DNA binding

Region

420 – 429

10

Involved in primer binding By similarity

Region

466 – 505

40

DNA binding

Sites

Active site

312

1

Schiff-base intermediate with DNA

Metal binding

427

1

Manganese By similarity

Metal binding

429

1

Manganese By similarity

Metal binding

490

1

Manganese By similarity

Natural variations

Natural variant

221

1

T → P.
Corresponds to variant rs3730463 [ dbSNP | Ensembl ].

VAR_020268

Natural variant

438

1

R → W. Ref.4
Corresponds to variant rs3730477 [ dbSNP | Ensembl ].

VAR_020269

Experimental info

Mutagenesis

312

1

K → A: Reduces dRP lyase activity by over 90%. Ref.9

Mutagenesis

505

1

Y → A: No effect on polymerase activity. Reduces terminal transferase activitites. Ref.11

Mutagenesis

506

1

F → G or R: Strongly reduces polymerase and terminal transferase activitites. Ref.11

Sequence conflict

138

1

Y → C in AAG22519. Ref.3

Sequence conflict

298

1

E → G in AAH68529. Ref.7

Secondary structure

1

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575

Helix Strand Turn

Details...

Helix

37 – 39

3

Helix

41 – 43

3

Turn

50 – 52

3

Beta strand

55 – 57

3

Helix

60 – 67

8

Beta strand

82 – 85

4

Beta strand

87 – 89

3

Helix

91 – 97

7

Beta strand

108 – 111

4

Helix

112 – 120

9

Helix

127 – 129

3

Beta strand

247 – 250

4

Helix

254 – 269

16

Helix

273 – 287

15

Beta strand

289 – 291

3

Helix

296 – 300

5

Helix

307 – 318

12

Beta strand

319 – 321

3

Helix

323 – 327

5

Helix

332 – 339

8

Helix

346 – 354

9

Helix

360 – 366

7

Helix

371 – 378

8

Turn

379 – 381

3

Helix

382 – 384

3

Helix

389 – 404

16

Beta strand

411 – 414

4

Helix

416 – 419

4

Beta strand

423 – 433

11

Beta strand

435 – 438

4

Turn

439 – 442

4

Helix

444 – 453

10

Beta strand

457 – 462

6

Beta strand

466 – 468

3

Beta strand

472 – 477

6

Beta strand

480 – 483

4

Beta strand

487 – 493

7

Helix

496 – 498

3

Helix

499 – 507

9

Helix

510 – 522

13

Beta strand

525 – 527

3

Beta strand

532 – 535

4

Beta strand

544 – 546

3

Beta strand

549 – 551

3

Helix

556 – 562

7

Helix

570 – 573

4

Sequences

	Sequence		Length	Mass (Da)
	Q9UGP5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FD9196A1C94923C4	FASTA	575	63,482
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

NIEHS-SNPs

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.

IPI

IPI00002284.

RefSeq

NP_001167555.1. NM_001174084.1.
NP_001167556.1. NM_001174085.1.
NP_037406.1. NM_013274.3.

UniGene

Hs.523230.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9UGP5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48999N.

MINT

MINT-3079892.

STRING

9606.ENSP00000299206.

PTM databases

PhosphoSite

Q9UGP5.

Polymorphism databases

DMDM

17367126.

Proteomic databases

PaxDb

Q9UGP5.

PRIDE

Q9UGP5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299206; ENSP00000299206; ENSG00000166169.
ENST00000370162; ENSP00000359181; ENSG00000166169.
ENST00000370169; ENSP00000359188; ENSG00000166169.

GeneID

27343.

KEGG

hsa:27343.

UCSC

uc001ktg.1. human.

Organism-specific databases

CTD

27343.

GeneCards

GC10M103328.

HGNC

HGNC:9184. POLL.

MIM

606343. gene.

neXtProt

NX_Q9UGP5.

PharmGKB

PA33504.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1796.

HOGENOM

HOG000007787.

HOVERGEN

HBG002788.

InParanoid

Q9UGP5.

KO

K03512.

OMA

YQQGFRT.

OrthoDB

EOG4XWFXM.

PhylomeDB

Q9UGP5.

Enzyme and pathway databases

SABIO-RK

Q9UGP5.

Gene expression databases

ArrayExpress

Q9UGP5.

Bgee

Q9UGP5.

CleanEx

HS_POLL.

Genevestigator

Q9UGP5.

GermOnline

ENSG00000166169. Homo sapiens.

Family and domain databases

InterPro

IPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR002008. DNA_pol_X_beta-like.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
[Graphical view]

Pfam

PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]

PRINTS

PR00869. DNAPOLX.
PR00870. DNAPOLXBETA.

SMART

SM00278. HhH1. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF81585. DNA_pol_lambd_fingers_domain. 1 hit.
SSF47802. DNApol_B_N_like. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9UGP5.

ChEMBL

CHEMBL5367.

EvolutionaryTrace

Q9UGP5.

GenomeRNAi

27343.

NextBio

50422.

SOURCE

Search...

Entry information

Entry name

DPOLL_HUMAN

Accession

Primary (citable) accession number: Q9UGP5
Secondary accession number(s): D3DR76 , Q5JQP5, Q6NUM2, Q9HA10, Q9HB35

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.