Skip Header

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

Q9UNA4 - POLI_HUMAN

UniProt

Q9UNA4 - POLI_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA polymerase iota

Gene

POLI

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

Functioni

Error-prone 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. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.7 Publications

Catalytic activityi

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

Cofactori

Mg2+

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Magnesium
Binding sitei64 – 641dNTP
Binding sitei96 – 961dNTP
Metal bindingi151 – 1511Magnesium
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA repair Source: ProtInc
  2. DNA replication Source: UniProtKB-KW
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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase iota (EC:2.7.7.7)
Alternative name(s):
Eta2
RAD30 homolog B
Gene namesi
Name:POLI
Synonyms:RAD30B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:9182. POLI.

Subcellular locationi

Nucleus 1 Publication
Note: Accumulates at replication forks after DNA damage.

GO - Cellular componenti

  1. intracellular Source: LIFEdb
  2. intracellular membrane-bounded organelle Source: HPA
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740DNA polymerase iotaPRO_0000173988Add
BLAST

Proteomic databases

MaxQBiQ9UNA4.
PaxDbiQ9UNA4.
PRIDEiQ9UNA4.

PTM databases

PhosphoSiteiQ9UNA4.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in testis.2 Publications

Gene expression databases

BgeeiQ9UNA4.
CleanExiHS_POLI.
ExpressionAtlasiQ9UNA4. baseline and differential.
GenevestigatoriQ9UNA4.

Organism-specific databases

HPAiHPA012000.

Interactioni

Subunit structurei

Interacts with REV1 (By similarity). Interacts with POLH.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAZAP2Q150383EBI-741774,EBI-724310
PCNAQ6FI352EBI-741774,EBI-8469539
UBCP0CG484EBI-741774,EBI-3390054
XRCC1P188872EBI-741774,EBI-947466

Protein-protein interaction databases

BioGridi116370. 16 interactions.
IntActiQ9UNA4. 12 interactions.
MINTiMINT-1189678.
STRINGi9606.ENSP00000217800.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 606Combined sources
Helixi63 – 719Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 915Combined sources
Helixi93 – 964Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1054Combined sources
Helixi106 – 1127Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 1204Combined sources
Helixi125 – 14117Combined sources
Beta strandi145 – 1484Combined sources
Turni149 – 1513Combined sources
Beta strandi152 – 1565Combined sources
Helixi158 – 16710Combined sources
Beta strandi170 – 1723Combined sources
Helixi173 – 1753Combined sources
Beta strandi180 – 1823Combined sources
Helixi183 – 1853Combined sources
Helixi193 – 21624Combined sources
Beta strandi220 – 2278Combined sources
Helixi228 – 2358Combined sources
Beta strandi236 – 2383Combined sources
Turni239 – 2413Combined sources
Beta strandi243 – 2453Combined sources
Helixi248 – 2503Combined sources
Helixi251 – 2577Combined sources
Helixi261 – 2633Combined sources
Helixi269 – 2779Combined sources
Helixi283 – 2886Combined sources
Helixi291 – 31020Combined sources
Beta strandi325 – 3328Combined sources
Turni334 – 3363Combined sources
Beta strandi339 – 3413Combined sources
Helixi342 – 36019Combined sources
Beta strandi362 – 37413Combined sources
Turni377 – 3793Combined sources
Beta strandi383 – 3886Combined sources
Turni391 – 3933Combined sources
Beta strandi397 – 3993Combined sources
Helixi401 – 4044Combined sources
Helixi405 – 41915Combined sources
Beta strandi422 – 4243Combined sources
Beta strandi427 – 43913Combined sources
Beta strandi704 – 7074Combined sources
Helixi710 – 7134Combined sources
Helixi718 – 73114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3NX-ray2.30A/B52-439[»]
1ZETX-ray2.30A52-439[»]
2ALZX-ray2.50A50-439[»]
2DPIX-ray2.30A26-445[»]
2DPJX-ray2.30A26-445[»]
2FLLX-ray2.60A26-445[»]
2FLNX-ray2.50A26-445[»]
2FLPX-ray2.40A26-445[»]
2KHUNMR-A697-740[»]
2KHWNMR-A697-740[»]
2KTFNMR-B704-730[»]
2L0FNMR-B699-740[»]
2L0GNMR-A704-730[»]
2MBBNMR-A516-555[»]
3EPGX-ray2.50A26-445[»]
3EPIX-ray2.90A26-445[»]
3G6VX-ray2.20A26-445[»]
3G6XX-ray2.08A26-445[»]
3G6YX-ray2.10A26-445[»]
3GV5X-ray2.00B/D26-445[»]
3GV7X-ray2.20B26-445[»]
3GV8X-ray2.00B26-445[»]
3H40X-ray2.30A51-439[»]
3H4BX-ray2.85A50-439[»]
3H4DX-ray2.20A50-439[»]
3NGDX-ray2.80A26-445[»]
3OSNX-ray1.90A26-445[»]
3Q8PX-ray1.95B26-445[»]
3Q8QX-ray2.03B26-445[»]
3Q8RX-ray2.45B26-445[»]
3Q8SX-ray2.09B26-445[»]
4EBCX-ray2.90A26-445[»]
4EBDX-ray2.57A26-445[»]
4EBEX-ray2.10A26-445[»]
4EYHX-ray2.90B26-445[»]
4EYIX-ray2.90B26-445[»]
4FS1X-ray2.50A26-445[»]
4FS2X-ray2.05A26-445[»]
ProteinModelPortaliQ9UNA4.
SMRiQ9UNA4. Positions 52-439, 519-555, 701-732.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UNA4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 268214UmuCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 3328DNA binding
Regioni368 – 38619DNA bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi589 – 61729Ser-richAdd
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 1 umuC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000234325.
HOVERGENiHBG053634.
InParanoidiQ9UNA4.
KOiK03510.
OMAiCFCNLKA.
OrthoDBiEOG7C8GGJ.
PhylomeDBiQ9UNA4.
TreeFamiTF324222.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UNA4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEKLGVEPEE EGGGDDDEED AEAWAMELAD VGAAASSQGV HDQVLPTPNA 
        60         70         80         90        100
SSRVIVHVDL DCFYAQVEMI SNPELKDKPL GVQQKYLVVT CNYEARKLGV 
       110        120        130        140        150
KKLMNVRDAK EKCPQLVLVN GEDLTRYREM SYKVTELLEE FSPVVERLGF 
       160        170        180        190        200
DENFVDLTEM VEKRLQQLQS DELSAVTVSG HVYNNQSINL LDVLHIRLLV 
       210        220        230        240        250
GSQIAAEMRE AMYNQLGLTG CAGVASNKLL AKLVSGVFKP NQQTVLLPES 
       260        270        280        290        300
CQHLIHSLNH IKEIPGIGYK TAKCLEALGI NSVRDLQTFS PKILEKELGI 
       310        320        330        340        350
SVAQRIQKLS FGEDNSPVIL SGPPQSFSEE DSFKKCSSEV EAKNKIEELL 
       360        370        380        390        400
ASLLNRVCQD GRKPHTVRLI IRRYSSEKHY GRESRQCPIP SHVIQKLGTG 
       410        420        430        440        450
NYDVMTPMVD ILMKLFRNMV NVKMPFHLTL LSVCFCNLKA LNTAKKGLID 
       460        470        480        490        500
YYLMPSLSTT SRSGKHSFKM KDTHMEDFPK DKETNRDFLP SGRIESTRTR 
       510        520        530        540        550
ESPLDTTNFS KEKDINEFPL CSLPEGVDQE VFKQLPVDIQ EEILSGKSRE 
       560        570        580        590        600
KFQGKGSVSC PLHASRGVLS FFSKKQMQDI PINPRDHLSS SKQVSSVSPC 
       610        620        630        640        650
EPGTSGFNSS SSSYMSSQKD YSYYLDNRLK DERISQGPKE PQGFHFTNSN 
       660        670        680        690        700
PAVSAFHSFP NLQSEQLFSR NHTTDSHKQT VATDSHEGLT ENREPDSVDE 
       710        720        730        740
KITFPSDIDP QVFYELPEAV QKELLAEWKR AGSDFHIGHK
Length:740
Mass (Da):83,006
Last modified:April 5, 2011 - v3
Checksum:iC1A5BF0894E91FDF
GO

Sequence cautioni

The sequence AAD50381.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF63383.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH32662.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM11872.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB66605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing in AAD50381. (PubMed:10458907)Curated
Sequence conflicti15 – 151Missing in CAB66605. (PubMed:11230166)Curated
Sequence conflicti15 – 151Missing in AAF63383. 1 PublicationCurated
Sequence conflicti337 – 3371S → T in CAB66605. (PubMed:11230166)Curated
Sequence conflicti433 – 4331V → A in AAF63383. 1 PublicationCurated
Sequence conflicti514 – 5141D → G in AAF63383. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961R → G.1 Publication
Corresponds to variant rs3218778 [ dbSNP | Ensembl ].		VAR_021239
Natural varianti261 – 2611I → M.1 Publication
Corresponds to variant rs3218784 [ dbSNP | Ensembl ].		VAR_021240
Natural varianti276 – 2761E → K.1 Publication
Corresponds to variant rs3218783 [ dbSNP | Ensembl ].		VAR_021241
Natural varianti474 – 4741H → R.1 Publication
Corresponds to variant rs3730823 [ dbSNP | Ensembl ].		VAR_021242
Natural varianti532 – 5321F → S.2 Publications
Corresponds to variant rs3218786 [ dbSNP | Ensembl ].		VAR_021243
Natural varianti560 – 5601C → R.1 Publication
Corresponds to variant rs3218787 [ dbSNP | Ensembl ].		VAR_021244
Natural varianti731 – 7311A → T.2 Publications
Corresponds to variant rs8305 [ dbSNP | Ensembl ].		VAR_021245

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY094607 Genomic DNA. Translation: AAM11872.1. Sequence problems.
AC093462 Genomic DNA. No translation available.
AF140501 mRNA. Translation: AAD50381.1. Different initiation.
AL136670 mRNA. Translation: CAB66605.1. Different initiation.
BC032662 mRNA. Translation: AAH32662.1. Different initiation.
AF245438 mRNA. Translation: AAF63383.1. Different initiation.
CCDSiCCDS11954.2.
RefSeqiNP_009126.2. NM_007195.2.
UniGeneiHs.438533.

Genome annotation databases

EnsembliENST00000579534; ENSP00000462664; ENSG00000101751.
GeneIDi11201.
KEGGihsa:11201.
UCSCiuc002lfj.4. human.

Polymorphism databases

DMDMi327478565.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY094607 Genomic DNA. Translation: AAM11872.1. Sequence problems.
AC093462 Genomic DNA. No translation available.
AF140501 mRNA. Translation: AAD50381.1. Different initiation.
AL136670 mRNA. Translation: CAB66605.1. Different initiation.
BC032662 mRNA. Translation: AAH32662.1. Different initiation.
AF245438 mRNA. Translation: AAF63383.1. Different initiation.
CCDSiCCDS11954.2.
RefSeqiNP_009126.2. NM_007195.2.
UniGeneiHs.438533.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3NX-ray2.30A/B52-439[»]
1ZETX-ray2.30A52-439[»]
2ALZX-ray2.50A50-439[»]
2DPIX-ray2.30A26-445[»]
2DPJX-ray2.30A26-445[»]
2FLLX-ray2.60A26-445[»]
2FLNX-ray2.50A26-445[»]
2FLPX-ray2.40A26-445[»]
2KHUNMR-A697-740[»]
2KHWNMR-A697-740[»]
2KTFNMR-B704-730[»]
2L0FNMR-B699-740[»]
2L0GNMR-A704-730[»]
2MBBNMR-A516-555[»]
3EPGX-ray2.50A26-445[»]
3EPIX-ray2.90A26-445[»]
3G6VX-ray2.20A26-445[»]
3G6XX-ray2.08A26-445[»]
3G6YX-ray2.10A26-445[»]
3GV5X-ray2.00B/D26-445[»]
3GV7X-ray2.20B26-445[»]
3GV8X-ray2.00B26-445[»]
3H40X-ray2.30A51-439[»]
3H4BX-ray2.85A50-439[»]
3H4DX-ray2.20A50-439[»]
3NGDX-ray2.80A26-445[»]
3OSNX-ray1.90A26-445[»]
3Q8PX-ray1.95B26-445[»]
3Q8QX-ray2.03B26-445[»]
3Q8RX-ray2.45B26-445[»]
3Q8SX-ray2.09B26-445[»]
4EBCX-ray2.90A26-445[»]
4EBDX-ray2.57A26-445[»]
4EBEX-ray2.10A26-445[»]
4EYHX-ray2.90B26-445[»]
4EYIX-ray2.90B26-445[»]
4FS1X-ray2.50A26-445[»]
4FS2X-ray2.05A26-445[»]
ProteinModelPortaliQ9UNA4.
SMRiQ9UNA4. Positions 52-439, 519-555, 701-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116370. 16 interactions.
IntActiQ9UNA4. 12 interactions.
MINTiMINT-1189678.
STRINGi9606.ENSP00000217800.

Chemistry

ChEMBLiCHEMBL5391.

PTM databases

PhosphoSiteiQ9UNA4.

Polymorphism databases

DMDMi327478565.

Proteomic databases

MaxQBiQ9UNA4.
PaxDbiQ9UNA4.
PRIDEiQ9UNA4.

Protocols and materials databases

DNASUi11201.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000579534; ENSP00000462664; ENSG00000101751.
GeneIDi11201.
KEGGihsa:11201.
UCSCiuc002lfj.4. human.

Organism-specific databases

CTDi11201.
GeneCardsiGC18P051795.
H-InvDBHIX0014457.
HGNCiHGNC:9182. POLI.
HPAiHPA012000.
MIMi605252. gene.
neXtProtiNX_Q9UNA4.
PharmGKBiPA33502.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000234325.
HOVERGENiHBG053634.
InParanoidiQ9UNA4.
KOiK03510.
OMAiCFCNLKA.
OrthoDBiEOG7C8GGJ.
PhylomeDBiQ9UNA4.
TreeFamiTF324222.

Miscellaneous databases

ChiTaRSiPOLI. human.
EvolutionaryTraceiQ9UNA4.
GeneWikiiPOLI.
GenomeRNAii11201.
NextBioi42637.
PROiQ9UNA4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UNA4.
CleanExiHS_POLI.
ExpressionAtlasiQ9UNA4. baseline and differential.
GenevestigatoriQ9UNA4.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIEHS SNPs program
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-96; MET-261; LYS-276; ARG-474; SER-532 AND ARG-560.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta."
    McDonald J.P., Rapic-Otrin V., Epstein J.A., Broughton B.C., Wang X., Lehmann A.R., Wolgemuth D.J., Woodgate R.
    Genomics 60:20-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-740, VARIANT THR-731, TISSUE SPECIFICITY.
    Tissue: Umbilical vein endothelial cell.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-740, VARIANT SER-532.
    Tissue: Brain.
  5. "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 12-740.
    Tissue: Uterus.
  6. "Human eta2 gene homologous to bacterial UmuC and Rev1 genes."
    Poltoratsky V.P., Scharff M.D.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-740, VARIANT THR-731.
  7. "Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota."
    Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R.
    EMBO J. 19:5259-5266(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "5'-deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro."
    Bebenek K., Tissier A., Frank E.G., McDonald J.P., Prasad R., Wilson S.H., Woodgate R., Kunkel T.A.
    Science 291:2156-2159(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SCHIFF BASE FORMATION.
  9. "Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template."
    Frank E.G., Tissier A., McDonald J.P., Rapic-Otrin V., Zeng X., Gearhart P.J., Woodgate R.
    EMBO J. 20:2914-2922(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota."
    Faili A., Aoufouchi S., Flatter E., Gueranger Q., Reynaud C.-A., Weill J.-C.
    Nature 419:944-947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells."
    Kannouche P.L., Fernandez de Henestrosa A.R., Coull B., Vidal A.E., Gray C., Zicha D., Woodgate R., Lehmann A.R.
    EMBO J. 22:1223-1233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH POLH.
  12. "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.
  13. "Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa."
    Washington M.T., Minko I.G., Johnson R.E., Wolfle W.T., Harris T.M., Lloyd R.S., Prakash S., Prakash L.
    Mol. Cell. Biol. 24:5687-5693(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing."
    Nair D.T., Johnson R.E., Prakash S., Prakash L., Aggarwal A.K.
    Nature 430:377-380(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 52-439 IN COMPLEX WITH DNA AND NUCLEOTIDE, FUNCTION.
+Additional computationally mapped references.

Entry informationi

Entry nameiPOLI_HUMAN
AccessioniPrimary (citable) accession number: Q9UNA4
Secondary accession number(s): Q8N590, Q9H0S1, Q9NYH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: April 5, 2011
Last modified: February 4, 2015
This is version 125 of the entry and version 3 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 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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