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Protein

DNA polymerase kappa

Gene

POLK

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

Functioni

DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.7 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations. Prefers Mg2+, but can also use Mn2+.1 Publication

pH dependencei

Optimum pH is 6.5-7.5.

Temperature dependencei

Optimum temperature is 37 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071MagnesiumBy similarity
Metal bindingi198 – 1981MagnesiumBy similarity
Metal bindingi199 – 1991MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 64727UBZ-type 1Add
BLAST
Zinc fingeri776 – 80227UBZ-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, DNA synthesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Schiff base, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase kappa (EC:2.7.7.7)
Alternative name(s):
DINB protein
Short name:
DINP
Gene namesi
Name:POLK
Synonyms:DINB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:9183. POLK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981D → A: Loss of DNA polymerase activity; when associated with A-199. 1 Publication
Mutagenesisi199 – 1991E → A: Loss of DNA polymerase activity; when associated with D-198. 1 Publication

Organism-specific databases

PharmGKBiPA33503.

Chemistry

ChEMBLiCHEMBL5365.

Polymorphism and mutation databases

BioMutaiPOLK.
DMDMi59798438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870DNA polymerase kappaPRO_0000173990Add
BLAST

Proteomic databases

EPDiQ9UBT6.
MaxQBiQ9UBT6.
PaxDbiQ9UBT6.
PRIDEiQ9UBT6.

PTM databases

iPTMnetiQ9UBT6.
PhosphoSiteiQ9UBT6.

Expressioni

Tissue specificityi

Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiQ9UBT6.
ExpressionAtlasiQ9UBT6. baseline and differential.
GenevisibleiQ9UBT6. HS.

Interactioni

Subunit structurei

Interacts with REV1 (By similarity). Interacts with PCNA.By similarity1 Publication

Protein-protein interaction databases

BioGridi119532. 43 interactions.
IntActiQ9UBT6. 26 interactions.
STRINGi9606.ENSP00000241436.

Chemistry

BindingDBiQ9UBT6.

Structurei

Secondary structure

1
870
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4412Combined sources
Helixi48 – 7225Combined sources
Helixi78 – 9417Combined sources
Beta strandi103 – 1086Combined sources
Helixi111 – 1199Combined sources
Helixi121 – 1233Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi136 – 1394Combined sources
Helixi141 – 1455Combined sources
Helixi154 – 1607Combined sources
Beta strandi165 – 1673Combined sources
Helixi171 – 18818Combined sources
Beta strandi196 – 2038Combined sources
Helixi205 – 2117Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2224Combined sources
Helixi236 – 2416Combined sources
Turni243 – 2486Combined sources
Helixi249 – 2513Combined sources
Beta strandi283 – 2853Combined sources
Helixi290 – 30516Combined sources
Beta strandi309 – 3168Combined sources
Helixi317 – 32610Combined sources
Turni327 – 3304Combined sources
Beta strandi332 – 3343Combined sources
Helixi339 – 3468Combined sources
Helixi351 – 3533Combined sources
Helixi359 – 3679Combined sources
Helixi373 – 3786Combined sources
Helixi380 – 3867Combined sources
Helixi389 – 39911Combined sources
Beta strandi416 – 42510Combined sources
Helixi428 – 43912Combined sources
Turni448 – 4503Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi467 – 4704Combined sources
Helixi484 – 49613Combined sources
Beta strandi497 – 4993Combined sources
Beta strandi506 – 5138Combined sources
Helixi567 – 5748Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T94X-ray2.40A/B68-526[»]
2LSINMR-B562-577[»]
2OH2X-ray3.05A/B19-526[»]
2W7OX-ray3.16A/B19-526[»]
2W7PX-ray3.71A/B19-526[»]
3IN5X-ray3.20A/B19-526[»]
3PZPX-ray3.34A/B19-528[»]
4BA9X-ray2.73A/B/C/D/E/F563-575[»]
4GK5X-ray3.21G564-573[»]
4U6PX-ray2.59A/B1-526[»]
4U7CX-ray2.80A/B27-518[»]
ProteinModelPortaliQ9UBT6.
SMRiQ9UBT6. Positions 21-517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBT6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 358256UmuCAdd
BLAST

Domaini

The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.

Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated
Contains 2 UBZ-type zinc fingers.Curated
Contains 1 umuC domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri621 – 64727UBZ-type 1Add
BLAST
Zinc fingeri776 – 80227UBZ-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2094. Eukaryota.
COG0389. LUCA.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000082711.
HOVERGENiHBG101212.
InParanoidiQ9UBT6.
KOiK03511.
OMAiNWPEDKR.
OrthoDBiEOG73Z2SP.
PhylomeDBiQ9UBT6.
TreeFamiTF314387.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
HAMAPiMF_01113. DNApol_IV.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
IPR001126. UmuC.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view]
SMARTiSM00734. ZnF_Rad18. 2 hits.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBT6-1) [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
MDSTKEKCDS YKDDLLLRMG LNDNKAGMEG LDKEKINKII MEATKGSRFY
60 70 80 90 100
GNELKKEKQV NQRIENMMQQ KAQITSQQLR KAQLQVDRFA MELEQSRNLS
110 120 130 140 150
NTIVHIDMDA FYAAVEMRDN PELKDKPIAV GSMSMLSTSN YHARRFGVRA
160 170 180 190 200
AMPGFIAKRL CPQLIIVPPN FDKYRAVSKE VKEILADYDP NFMAMSLDEA
210 220 230 240 250
YLNITKHLEE RQNWPEDKRR YFIKMGSSVE NDNPGKEVNK LSEHERSISP
260 270 280 290 300
LLFEESPSDV QPPGDPFQVN FEEQNNPQIL QNSVVFGTSA QEVVKEIRFR
310 320 330 340 350
IEQKTTLTAS AGIAPNTMLA KVCSDKNKPN GQYQILPNRQ AVMDFIKDLP
360 370 380 390 400
IRKVSGIGKV TEKMLKALGI ITCTELYQQR ALLSLLFSET SWHYFLHISL
410 420 430 440 450
GLGSTHLTRD GERKSMSVER TFSEINKAEE QYSLCQELCS ELAQDLQKER
460 470 480 490 500
LKGRTVTIKL KNVNFEVKTR ASTVSSVVST AEEIFAIAKE LLKTEIDADF
510 520 530 540 550
PHPLRLRLMG VRISSFPNEE DRKHQQRSII GFLQAGNQAL SATECTLEKT
560 570 580 590 600
DKDKFVKPLE MSHKKSFFDK KRSERKWSHQ DTFKCEAVNK QSFQTSQPFQ
610 620 630 640 650
VLKKKMNENL EISENSDDCQ ILTCPVCFRA QGCISLEALN KHVDECLDGP
660 670 680 690 700
SISENFKMFS CSHVSATKVN KKENVPASSL CEKQDYEAHP KIKEISSVDC
710 720 730 740 750
IALVDTIDNS SKAESIDALS NKHSKEECSS LPSKSFNIEH CHQNSSSTVS
760 770 780 790 800
LENEDVGSFR QEYRQPYLCE VKTGQALVCP VCNVEQKTSD LTLFNVHVDV
810 820 830 840 850
CLNKSFIQEL RKDKFNPVNQ PKESSRSTGS SSGVQKAVTR TKRPGLMTKY
860 870
STSKKIKPNN PKHTLDIFFK
Length:870
Mass (Da):98,809
Last modified:May 1, 2000 - v1
Checksum:i40CB259A65F6A796
GO
Isoform 2 (identifier: Q9UBT6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     453-472: GRTVTIKLKNVNFEVKTRAS → VLYFDMVSLVFKFFNSKMLP
     473-870: Missing.

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):54,132
Checksum:i45D26D63D90D0225
GO
Isoform 3 (identifier: Q9UBT6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-509: Missing.

Show »
Length:672
Mass (Da):76,454
Checksum:iD5BADE5559C88977
GO
Isoform 4 (identifier: Q9UBT6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     453-462: GRTVTIKLKN → KKYLPLLRNC
     463-870: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Show »
Length:372
Mass (Da):42,487
Checksum:iFFDC64B0DC9D2A35
GO
Isoform 5 (identifier: Q9UBT6-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     453-489: GRTVTIKLKNVNFEVKTRASTVSSVVSTAEEIFAIAK → VFGYLVFPMKRTGNTNKGALLAFYRLETKPCQPLSVH
     490-870: Missing.

Show »
Length:489
Mass (Da):55,904
Checksum:iB3EA53A1890A1C9E
GO
Isoform 6 (identifier: Q9UBT6-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     453-461: GRTVTIKLK → VAQVEYRRL
     462-870: Missing.

Show »
Length:461
Mass (Da):52,839
Checksum:iF2D33767C82284BD
GO
Isoform 7 (identifier: Q9UBT6-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     453-461: GRTVTIKLK → VAQVEYRRL
     462-870: Missing.

Show »
Length:371
Mass (Da):42,372
Checksum:iB72DA3E0F14FD870
GO
Isoform 8 (identifier: Q9UBT6-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Show »
Length:780
Mass (Da):88,342
Checksum:iE36919BC4E7D4C84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211L → F in BAB58975 (Ref. 11) Curated
Sequence conflicti39 – 391I → T in BAB58975 (Ref. 11) Curated
Sequence conflicti219 – 2191R → L in BAB58976 (Ref. 11) Curated
Sequence conflicti342 – 3421V → G in BAC03714 (PubMed:14702039).Curated
Sequence conflicti557 – 5571K → N in AAF23270 (Ref. 4) Curated
Sequence conflicti847 – 8471M → V in AAF23270 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti423 – 4231S → R.
Corresponds to variant rs35257416 [ dbSNP | Ensembl ].
VAR_048886
Natural varianti595 – 5951T → I.1 Publication
Corresponds to variant rs5744713 [ dbSNP | Ensembl ].
VAR_021246
Natural varianti612 – 6121I → V.
Corresponds to variant rs3822587 [ dbSNP | Ensembl ].
VAR_021247
Natural varianti635 – 6351S → N.
Corresponds to variant rs35501530 [ dbSNP | Ensembl ].
VAR_048887
Natural varianti832 – 8321S → N.1 Publication
Corresponds to variant rs5744716 [ dbSNP | Ensembl ].
VAR_021248

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform 4, isoform 7 and isoform 8. 2 PublicationsVSP_012804Add
BLAST
Alternative sequencei312 – 509198Missing in isoform 3. 1 PublicationVSP_012803Add
BLAST
Alternative sequencei453 – 48937GRTVT…FAIAK → VFGYLVFPMKRTGNTNKGAL LAFYRLETKPCQPLSVH in isoform 5. 1 PublicationVSP_053406Add
BLAST
Alternative sequencei453 – 47220GRTVT…KTRAS → VLYFDMVSLVFKFFNSKMLP in isoform 2. 1 PublicationVSP_012801Add
BLAST
Alternative sequencei453 – 46210GRTVTIKLKN → KKYLPLLRNC in isoform 4. 1 PublicationVSP_012805
Alternative sequencei453 – 4619GRTVTIKLK → VAQVEYRRL in isoform 6 and isoform 7. 1 PublicationVSP_053407
Alternative sequencei462 – 870409Missing in isoform 6 and isoform 7. 1 PublicationVSP_053408Add
BLAST
Alternative sequencei463 – 870408Missing in isoform 4. 1 PublicationVSP_012806Add
BLAST
Alternative sequencei473 – 870398Missing in isoform 2. 1 PublicationVSP_012802Add
BLAST
Alternative sequencei490 – 870381Missing in isoform 5. 1 PublicationVSP_053409Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027564 mRNA. Translation: BAA86943.1.
AF163570 mRNA. Translation: AAF02540.1.
AY769929 mRNA. Translation: AAV80827.1.
AY769931 mRNA. Translation: AAV80829.1.
AY769930 mRNA. Translation: AAV80828.1.
AY769932 mRNA. Translation: AAV80830.1.
AF194973 mRNA. Translation: AAF23270.1.
AF315602 mRNA. Translation: AAN15780.1.
AF318313 mRNA. Translation: AAN15781.1.
AK091659 mRNA. Translation: BAC03714.1.
AK314610 mRNA. Translation: BAG37179.1.
AY273797 Genomic DNA. Translation: AAP12648.1.
AC010245 Genomic DNA. No translation available.
AC026424 Genomic DNA. No translation available.
AC116341 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95763.1.
BC014955 mRNA. Translation: AAH14955.1.
BC050718 mRNA. Translation: AAH50718.1.
AB036934 Genomic DNA. Translation: BAB58975.1.
AB036935 Genomic DNA. Translation: BAB58976.1.
CCDSiCCDS4030.1. [Q9UBT6-1]
RefSeqiNP_057302.1. NM_016218.2. [Q9UBT6-1]
XP_011541770.1. XM_011543468.1. [Q9UBT6-5]
UniGeneiHs.135756.

Genome annotation databases

EnsembliENST00000241436; ENSP00000241436; ENSG00000122008. [Q9UBT6-1]
ENST00000504026; ENSP00000425075; ENSG00000122008. [Q9UBT6-6]
ENST00000508526; ENSP00000426853; ENSG00000122008. [Q9UBT6-3]
ENST00000509126; ENSP00000423532; ENSG00000122008. [Q9UBT6-5]
ENST00000510815; ENSP00000422094; ENSG00000122008. [Q9UBT6-4]
ENST00000515295; ENSP00000424174; ENSG00000122008. [Q9UBT6-2]
GeneIDi51426.
KEGGihsa:51426.
UCSCiuc003kdw.4. human. [Q9UBT6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027564 mRNA. Translation: BAA86943.1.
AF163570 mRNA. Translation: AAF02540.1.
AY769929 mRNA. Translation: AAV80827.1.
AY769931 mRNA. Translation: AAV80829.1.
AY769930 mRNA. Translation: AAV80828.1.
AY769932 mRNA. Translation: AAV80830.1.
AF194973 mRNA. Translation: AAF23270.1.
AF315602 mRNA. Translation: AAN15780.1.
AF318313 mRNA. Translation: AAN15781.1.
AK091659 mRNA. Translation: BAC03714.1.
AK314610 mRNA. Translation: BAG37179.1.
AY273797 Genomic DNA. Translation: AAP12648.1.
AC010245 Genomic DNA. No translation available.
AC026424 Genomic DNA. No translation available.
AC116341 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95763.1.
BC014955 mRNA. Translation: AAH14955.1.
BC050718 mRNA. Translation: AAH50718.1.
AB036934 Genomic DNA. Translation: BAB58975.1.
AB036935 Genomic DNA. Translation: BAB58976.1.
CCDSiCCDS4030.1. [Q9UBT6-1]
RefSeqiNP_057302.1. NM_016218.2. [Q9UBT6-1]
XP_011541770.1. XM_011543468.1. [Q9UBT6-5]
UniGeneiHs.135756.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T94X-ray2.40A/B68-526[»]
2LSINMR-B562-577[»]
2OH2X-ray3.05A/B19-526[»]
2W7OX-ray3.16A/B19-526[»]
2W7PX-ray3.71A/B19-526[»]
3IN5X-ray3.20A/B19-526[»]
3PZPX-ray3.34A/B19-528[»]
4BA9X-ray2.73A/B/C/D/E/F563-575[»]
4GK5X-ray3.21G564-573[»]
4U6PX-ray2.59A/B1-526[»]
4U7CX-ray2.80A/B27-518[»]
ProteinModelPortaliQ9UBT6.
SMRiQ9UBT6. Positions 21-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119532. 43 interactions.
IntActiQ9UBT6. 26 interactions.
STRINGi9606.ENSP00000241436.

Chemistry

BindingDBiQ9UBT6.
ChEMBLiCHEMBL5365.

PTM databases

iPTMnetiQ9UBT6.
PhosphoSiteiQ9UBT6.

Polymorphism and mutation databases

BioMutaiPOLK.
DMDMi59798438.

Proteomic databases

EPDiQ9UBT6.
MaxQBiQ9UBT6.
PaxDbiQ9UBT6.
PRIDEiQ9UBT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241436; ENSP00000241436; ENSG00000122008. [Q9UBT6-1]
ENST00000504026; ENSP00000425075; ENSG00000122008. [Q9UBT6-6]
ENST00000508526; ENSP00000426853; ENSG00000122008. [Q9UBT6-3]
ENST00000509126; ENSP00000423532; ENSG00000122008. [Q9UBT6-5]
ENST00000510815; ENSP00000422094; ENSG00000122008. [Q9UBT6-4]
ENST00000515295; ENSP00000424174; ENSG00000122008. [Q9UBT6-2]
GeneIDi51426.
KEGGihsa:51426.
UCSCiuc003kdw.4. human. [Q9UBT6-1]

Organism-specific databases

CTDi51426.
GeneCardsiPOLK.
HGNCiHGNC:9183. POLK.
MIMi605650. gene.
neXtProtiNX_Q9UBT6.
PharmGKBiPA33503.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2094. Eukaryota.
COG0389. LUCA.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000082711.
HOVERGENiHBG101212.
InParanoidiQ9UBT6.
KOiK03511.
OMAiNWPEDKR.
OrthoDBiEOG73Z2SP.
PhylomeDBiQ9UBT6.
TreeFamiTF314387.

Enzyme and pathway databases

ReactomeiR-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

EvolutionaryTraceiQ9UBT6.
GeneWikiiPOLK.
GenomeRNAii51426.
PROiQ9UBT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBT6.
ExpressionAtlasiQ9UBT6. baseline and differential.
GenevisibleiQ9UBT6. HS.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
HAMAPiMF_01113. DNApol_IV.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
IPR001126. UmuC.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view]
SMARTiSM00734. ZnF_Rad18. 2 hits.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB."
    Ogi T., Kato T. Jr., Kato R., Ohmori H.
    Genes Cells 4:607-618(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily."
    Gerlach V.L., Aravind L., Gotway G., Schultz R.A., Koonin E.V., Friedberg E.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:11922-11927(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  3. "Multiple PolK (POLK) transcripts in mammalian testis."
    Guo C., Gao T., Confer N., Velasco-Miguel S., Friedberg E.C.
    DNA Repair 4:397-402(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE SPLICING.
    Tissue: Testis.
  4. "Homo sapiens DINP protein mRNA, complete cds."
    Poltoratsky V.P., Scharff M.D.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "A bidirectional promoter for the genes encoding DNA polymerase kappa and Goodpasture autoantigen binding protein: identification of a novel pol kappa alternative spliced variant."
    Revert-Ros F., Saus J.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  6. "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] (ISOFORMS 1 AND 4).
    Tissue: Brain and Trachea.
  7. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-595 AND ASN-832.
  8. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] OF 1-313 (ISOFORMS 1 AND 2).
    Tissue: Lymph and Spleen.
  11. "Homo sapiens genomic sequence, containing DINB1 gene."
    Ogi T., Yamamoto Y., Ohmori H.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231.
  12. "Purification and characterization of pol kappa, a DNA polymerase encoded by the human DINB1 gene."
    Gerlach V.L., Feaver W.J., Fischhaber P.L., Friedberg E.C.
    J. Biol. Chem. 276:92-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF ASP-198 AND GLU-199.
  13. "Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides."
    Fischhaber P.L., Gerlach V.L., Feaver W.J., Hatahet Z., Wallace S.S., Friedberg E.C.
    J. Biol. Chem. 277:37604-37611(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Localisation of human DNA polymerase kappa to replication foci."
    Bergoglio V., Bavoux C., Verbiest V., Hoffmann J.-S., Cazaux C.
    J. Cell Sci. 115:4413-4418(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA."
    Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L., Prakash S.
    Mol. Cell. Biol. 22:784-791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNA.
  16. "Role of human DNA polymerase kappa as an extender in translesion synthesis."
    Haracska L., Prakash L., Prakash S.
    Proc. Natl. Acad. Sci. U.S.A. 99:16000-16005(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Human DNA polymerase kappa uses template-primer misalignment as a novel means for extending mispaired termini and for generating single-base deletions."
    Wolfle W.T., Washington M.T., Prakash L., Prakash S.
    Genes Dev. 17:2191-2199(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair."
    Haracska L., Prakash L., Prakash S.
    Genes Dev. 17:2777-2785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SCHIFF BASE FORMATION.
  19. "Translesion synthesis past 2'-deoxyxanthosine, a nitric oxide-derived DNA adduct, by mammalian DNA polymerases."
    Yasui M., Suzuki N., Miller H., Matsuda T., Matsui S., Shibutani S.
    J. Mol. Biol. 344:665-674(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Crystal structure of the catalytic core of human DNA polymerase kappa."
    Uljon S.N., Johnson R.E., Edwards T.A., Prakash S., Prakash L., Aggarwal A.K.
    Structure 12:1395-1404(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 68-526.

Entry informationi

Entry nameiPOLK_HUMAN
AccessioniPrimary (citable) accession number: Q9UBT6
Secondary accession number(s): B2RBD2
, Q5Q9G5, Q5Q9G6, Q5Q9G7, Q5Q9G8, Q86VJ8, Q8IZY0, Q8IZY1, Q8NB30, Q96L01, Q96Q86, Q96Q87, Q9UHC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 136 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 5
    Human chromosome 5: 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

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 one 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.