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Q9Y253

- POLH_HUMAN

UniProt

Q9Y253 - POLH_HUMAN

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Protein

DNA polymerase eta

Gene

POLH

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.5 Publications

Catalytic activityi

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

Cofactori

Divalent metal cations. Prefers magnesium, but can also use manganese.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131MagnesiumPROSITE-ProRule annotation
Metal bindingi115 – 1151MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. DNA-dependent DNA replication Source: GOC
  2. DNA repair Source: Reactome
  3. DNA synthesis involved in DNA repair Source: UniProtKB
  4. postreplication repair Source: Ensembl
  5. pyrimidine dimer repair Source: Ensembl
  6. regulation of DNA repair Source: ProtInc
  7. response to UV-C Source: UniProtKB
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

Enzyme and pathway databases

SABIO-RKQ9Y253.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase eta (EC:2.7.7.7)
Alternative name(s):
RAD30 homolog A
Xeroderma pigmentosum variant type protein
Gene namesi
Name:POLH
Synonyms:RAD30, RAD30A, XPV
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9181. POLH.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum variant type (XPV) [MIM:278750]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. XPV shows normal nucleotide excision repair, but an exaggerated delay in recovery of replicative DNA synthesis. Most patients with the variant type of xeroderma pigmentosum do not develop clinical symptoms and skin neoplasias until a later age. Clinical manifestations are limited to photo-induced deterioration of the skin and eyes.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371Missing in XPV. 1 Publication
VAR_070835
Natural varianti75 – 751Missing in XPV; impairs translesion synthesis. 2 Publications
VAR_021226
Natural varianti93 – 931R → P in XPV. 1 Publication
VAR_070836
Natural varianti111 – 1111R → H in XPV.
VAR_021227
Natural varianti122 – 1221T → P in XPV. 1 Publication
VAR_021228
Natural varianti263 – 2631G → V in XPV; impairs translesion synthesis. 1 Publication
VAR_021230
Natural varianti266 – 2661V → D in XPV. 1 Publication
VAR_070837
Natural varianti295 – 2951G → R in XPV. 1 Publication
VAR_070838
Natural varianti361 – 3611R → S in XPV. 1 Publication
VAR_021232
Natural varianti535 – 5351K → E in XPV. 1 Publication
Corresponds to variant rs56307355 [ dbSNP | Ensembl ].
VAR_021234
Natural varianti589 – 5891K → T in XPV. 1 Publication
VAR_021236
Natural varianti692 – 6921T → A in XPV. 1 Publication
VAR_070839

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521Y → A or F: Reduces DNA polymerase activity. 1 Publication
Mutagenesisi52 – 521Y → E: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass. 1 Publication

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

MIMi278750. phenotype.
Orphaneti90342. Xeroderma pigmentosum variant.
PharmGKBiPA279.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713DNA polymerase etaPRO_0000173986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki682 – 682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki686 – 686Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki694 – 694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki709 – 709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitinated by RCHY1/PIRH2; ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions.2 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9Y253.
PaxDbiQ9Y253.
PRIDEiQ9Y253.

PTM databases

PhosphoSiteiQ9Y253.

Expressioni

Gene expression databases

BgeeiQ9Y253.
CleanExiHS_POLH.
ExpressionAtlasiQ9Y253. baseline and differential.
GenevestigatoriQ9Y253.

Organism-specific databases

HPAiHPA006721.
HPA026762.

Interactioni

Subunit structurei

Interacts with REV1. Interacts with monoubiquitinated PCNA, but not unmodified PCNA. Interacts with POLI. Interacts with PALB2 and BRCA2; the interactions are direct and are involved in POLH localization at collapsed replication forks and DNA polymerization activity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA2P515876EBI-2827270,EBI-79792
PALB2Q86YC27EBI-2827270,EBI-1222653
PCNAQ6FI353EBI-2827270,EBI-8469539
UBCP0CG484EBI-2827270,EBI-3390054

Protein-protein interaction databases

BioGridi111425. 20 interactions.
IntActiQ9Y253. 8 interactions.
MINTiMINT-2789553.
STRINGi9606.ENSP00000361310.

Structurei

Secondary structure

713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 33
Beta strandi9 – 146
Helixi17 – 259
Helixi27 – 293
Beta strandi34 – 385
Turni41 – 444
Beta strandi46 – 505
Helixi52 – 554
Turni56 – 583
Beta strandi61 – 644
Helixi65 – 717
Beta strandi76 – 794
Beta strandi81 – 833
Beta strandi86 – 883
Helixi90 – 10617
Beta strandi109 – 1135
Beta strandi116 – 1205
Helixi122 – 13211
Helixi139 – 1413
Beta strandi145 – 1473
Helixi159 – 1613
Helixi163 – 17715
Helixi186 – 20823
Beta strandi212 – 2198
Helixi220 – 22910
Turni230 – 2334
Beta strandi235 – 2373
Helixi240 – 2423
Helixi243 – 2486
Helixi252 – 2543
Helixi261 – 27010
Helixi275 – 2806
Helixi283 – 2908
Helixi292 – 30110
Turni302 – 3043
Beta strandi313 – 3153
Beta strandi319 – 3246
Helixi327 – 3293
Beta strandi331 – 3333
Helixi334 – 35926
Beta strandi360 – 37213
Beta strandi376 – 3783
Beta strandi380 – 3867
Helixi392 – 40312
Helixi404 – 4063
Beta strandi414 – 43118
Helixi532 – 5387
Beta strandi632 – 6343
Turni636 – 6383
Beta strandi641 – 6433
Helixi644 – 6463
Helixi647 – 65913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I5ONMR-A628-662[»]
2LSKNMR-B524-539[»]
3MR2X-ray1.83A1-432[»]
3MR3X-ray1.75A1-432[»]
3MR5X-ray1.80A1-432[»]
3MR6X-ray1.90A1-432[»]
3SI8X-ray2.15A1-432[»]
3TQ1X-ray2.56A1-432[»]
4DL2X-ray2.15A1-432[»]
4DL3X-ray2.10A1-432[»]
4DL4X-ray2.00A1-432[»]
4DL5X-ray2.92A1-432[»]
4DL6X-ray2.50A1-432[»]
4DL7X-ray1.97A1-432[»]
4ECQX-ray1.50A1-432[»]
4ECRX-ray1.89A1-432[»]
4ECSX-ray1.95A1-432[»]
4ECTX-ray1.80A1-432[»]
4ECUX-ray1.95A1-432[»]
4ECVX-ray1.52A1-432[»]
4ECWX-ray1.90A1-432[»]
4ECXX-ray1.74A1-432[»]
4ECYX-ray1.94A1-432[»]
4ECZX-ray1.83A1-432[»]
4ED0X-ray1.65A1-432[»]
4ED1X-ray1.81A1-432[»]
4ED2X-ray1.71A1-432[»]
4ED3X-ray1.79A1-432[»]
4ED6X-ray2.21A1-432[»]
4ED7X-ray1.72A1-432[»]
4ED8X-ray1.52A1-432[»]
4EEYX-ray2.32A1-432[»]
4J9KX-ray2.03A1-432[»]
4J9LX-ray1.85A1-432[»]
4J9MX-ray2.25A1-432[»]
4J9NX-ray1.96A1-432[»]
4J9OX-ray2.60A1-432[»]
4J9PX-ray2.30A1-432[»]
4J9QX-ray1.96A1-432[»]
4J9RX-ray2.35A1-432[»]
4J9SX-ray1.95A1-432[»]
4O3NX-ray1.58A1-432[»]
4O3OX-ray1.70A1-432[»]
4O3PX-ray1.72A1-432[»]
4O3QX-ray1.72A1-432[»]
4O3RX-ray1.62A1-432[»]
4O3SX-ray1.72A1-432[»]
4Q8EX-ray1.55A1-432[»]
4Q8FX-ray2.80A1-432[»]
ProteinModelPortaliQ9Y253.
SMRiQ9Y253. Positions 1-432, 629-662.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 259251UmuCPROSITE-ProRule annotationAdd
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.
HOGENOMiHOG000115605.
HOVERGENiHBG053633.
InParanoidiQ9Y253.
KOiK03509.
OMAiSPPLTML.
PhylomeDBiQ9Y253.
TreeFamiTF103010.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017061. DNA_pol_eta.
IPR017961. 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]
PIRSFiPIRSF036603. DPol_eta. 1 hit.
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y253) [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
MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV
60 70 80 90 100
SYEARAFGVT RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM
110 120 130 140 150
EIMSRFAVIE RASIDEAYVD LTSAVQERLQ KLQGQPISAD LLPSTYIEGL
160 170 180 190 200
PQGPTTAEET VQKEGMRKQG LFQWLDSLQI DNLTSPDLQL TVGAVIVEEM
210 220 230 240 250
RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH GSVPQLFSQM
260 270 280 290 300
PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA
310 320 330 340 350
MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE
360 370 380 390 400
RLTKDRNDND RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF
410 420 430 440 450
TVIKNCNTSG IQTEWSPPLT MLFLCATKFS ASAPSSSTDI TSFLSSDPSS
460 470 480 490 500
LPKVPVTSSE AKTQGSGPAV TATKKATTSL ESFFQKAAER QKVKEASLSS
510 520 530 540 550
LTAPTQAPMS NSPSKPSLPF QTSQSTGTEP FFKQKSLLLK QKQLNNSSVS
560 570 580 590 600
SPQQNPWSNC KALPNSLPTE YPGCVPVCEG VSKLEESSKA TPAEMDLAHN
610 620 630 640 650
SQSMHASSAS KSVLEVTQKA TPNPSLLAAE DQVPCEKCGS LVPVWDMPEH
660 670 680 690 700
MDYHFALELQ KSFLQPHSSN PQVVSAVSHQ GKRNPKSPLA CTNKRPRPEG
710
MQTLESFFKP LTH
Length:713
Mass (Da):78,413
Last modified:November 1, 1999 - v1
Checksum:i6D1D35A0F56ECE89
GO
Isoform 2 (identifier: Q9Y253-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     415-713: Missing.

Note: No experimental confirmation available.

Show »
Length:414
Mass (Da):46,283
Checksum:i9ABB24D0511A45EB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371Missing in XPV. 1 Publication
VAR_070835
Natural varianti75 – 751Missing in XPV; impairs translesion synthesis. 2 Publications
VAR_021226
Natural varianti93 – 931R → P in XPV. 1 Publication
VAR_070836
Natural varianti111 – 1111R → H in XPV.
VAR_021227
Natural varianti122 – 1221T → P in XPV. 1 Publication
VAR_021228
Natural varianti153 – 1531G → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036220
Natural varianti209 – 2091G → V.1 Publication
Corresponds to variant rs2307456 [ dbSNP | Ensembl ].
VAR_021229
Natural varianti263 – 2631G → V in XPV; impairs translesion synthesis. 1 Publication
VAR_021230
Natural varianti266 – 2661V → D in XPV. 1 Publication
VAR_070837
Natural varianti295 – 2951G → R in XPV. 1 Publication
VAR_070838
Natural varianti334 – 3341R → W.1 Publication
Corresponds to variant rs9333548 [ dbSNP | Ensembl ].
VAR_021231
Natural varianti361 – 3611R → S in XPV. 1 Publication
VAR_021232
Natural varianti478 – 4781T → M.1 Publication
Corresponds to variant rs9296419 [ dbSNP | Ensembl ].
VAR_021233
Natural varianti535 – 5351K → E in XPV. 1 Publication
Corresponds to variant rs56307355 [ dbSNP | Ensembl ].
VAR_021234
Natural varianti584 – 5841L → P.1 Publication
Corresponds to variant rs9333554 [ dbSNP | Ensembl ].
VAR_021235
Natural varianti589 – 5891K → T in XPV. 1 Publication
VAR_021236
Natural varianti595 – 5951M → V.1 Publication
Corresponds to variant rs9333555 [ dbSNP | Ensembl ].
VAR_021237
Natural varianti647 – 6471M → L.1 Publication
Corresponds to variant rs6941583 [ dbSNP | Ensembl ].
VAR_021238
Natural varianti692 – 6921T → A in XPV. 1 Publication
VAR_070839

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei415 – 713299Missing in isoform 2. 1 PublicationVSP_012799Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024313 mRNA. Translation: BAA81666.1.
AF158185 mRNA. Translation: AAD43810.1.
AB038008 Genomic DNA. Translation: BAB18601.1.
AY388614 Genomic DNA. Translation: AAQ81300.1.
AL353602, AL355802 Genomic DNA. Translation: CAI12786.1.
AL353602, AL355802 Genomic DNA. Translation: CAI12787.1.
AL355802, AL353602 Genomic DNA. Translation: CAI42641.1.
AL355802, AL353602 Genomic DNA. Translation: CAI42642.1.
BC015742 mRNA. Translation: AAH15742.1.
CCDSiCCDS4902.1. [Q9Y253-1]
RefSeqiNP_001278899.1. NM_001291970.1. [Q9Y253-2]
NP_006493.1. NM_006502.2. [Q9Y253-1]
UniGeneiHs.655467.

Genome annotation databases

EnsembliENST00000372226; ENSP00000361300; ENSG00000170734. [Q9Y253-2]
ENST00000372236; ENSP00000361310; ENSG00000170734. [Q9Y253-1]
GeneIDi5429.
KEGGihsa:5429.
UCSCiuc003ovq.4. human. [Q9Y253-1]

Polymorphism databases

DMDMi59798441.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Allelic variations of the XP genes
Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024313 mRNA. Translation: BAA81666.1 .
AF158185 mRNA. Translation: AAD43810.1 .
AB038008 Genomic DNA. Translation: BAB18601.1 .
AY388614 Genomic DNA. Translation: AAQ81300.1 .
AL353602 , AL355802 Genomic DNA. Translation: CAI12786.1 .
AL353602 , AL355802 Genomic DNA. Translation: CAI12787.1 .
AL355802 , AL353602 Genomic DNA. Translation: CAI42641.1 .
AL355802 , AL353602 Genomic DNA. Translation: CAI42642.1 .
BC015742 mRNA. Translation: AAH15742.1 .
CCDSi CCDS4902.1. [Q9Y253-1 ]
RefSeqi NP_001278899.1. NM_001291970.1. [Q9Y253-2 ]
NP_006493.1. NM_006502.2. [Q9Y253-1 ]
UniGenei Hs.655467.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I5O NMR - A 628-662 [» ]
2LSK NMR - B 524-539 [» ]
3MR2 X-ray 1.83 A 1-432 [» ]
3MR3 X-ray 1.75 A 1-432 [» ]
3MR5 X-ray 1.80 A 1-432 [» ]
3MR6 X-ray 1.90 A 1-432 [» ]
3SI8 X-ray 2.15 A 1-432 [» ]
3TQ1 X-ray 2.56 A 1-432 [» ]
4DL2 X-ray 2.15 A 1-432 [» ]
4DL3 X-ray 2.10 A 1-432 [» ]
4DL4 X-ray 2.00 A 1-432 [» ]
4DL5 X-ray 2.92 A 1-432 [» ]
4DL6 X-ray 2.50 A 1-432 [» ]
4DL7 X-ray 1.97 A 1-432 [» ]
4ECQ X-ray 1.50 A 1-432 [» ]
4ECR X-ray 1.89 A 1-432 [» ]
4ECS X-ray 1.95 A 1-432 [» ]
4ECT X-ray 1.80 A 1-432 [» ]
4ECU X-ray 1.95 A 1-432 [» ]
4ECV X-ray 1.52 A 1-432 [» ]
4ECW X-ray 1.90 A 1-432 [» ]
4ECX X-ray 1.74 A 1-432 [» ]
4ECY X-ray 1.94 A 1-432 [» ]
4ECZ X-ray 1.83 A 1-432 [» ]
4ED0 X-ray 1.65 A 1-432 [» ]
4ED1 X-ray 1.81 A 1-432 [» ]
4ED2 X-ray 1.71 A 1-432 [» ]
4ED3 X-ray 1.79 A 1-432 [» ]
4ED6 X-ray 2.21 A 1-432 [» ]
4ED7 X-ray 1.72 A 1-432 [» ]
4ED8 X-ray 1.52 A 1-432 [» ]
4EEY X-ray 2.32 A 1-432 [» ]
4J9K X-ray 2.03 A 1-432 [» ]
4J9L X-ray 1.85 A 1-432 [» ]
4J9M X-ray 2.25 A 1-432 [» ]
4J9N X-ray 1.96 A 1-432 [» ]
4J9O X-ray 2.60 A 1-432 [» ]
4J9P X-ray 2.30 A 1-432 [» ]
4J9Q X-ray 1.96 A 1-432 [» ]
4J9R X-ray 2.35 A 1-432 [» ]
4J9S X-ray 1.95 A 1-432 [» ]
4O3N X-ray 1.58 A 1-432 [» ]
4O3O X-ray 1.70 A 1-432 [» ]
4O3P X-ray 1.72 A 1-432 [» ]
4O3Q X-ray 1.72 A 1-432 [» ]
4O3R X-ray 1.62 A 1-432 [» ]
4O3S X-ray 1.72 A 1-432 [» ]
4Q8E X-ray 1.55 A 1-432 [» ]
4Q8F X-ray 2.80 A 1-432 [» ]
ProteinModelPortali Q9Y253.
SMRi Q9Y253. Positions 1-432, 629-662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111425. 20 interactions.
IntActi Q9Y253. 8 interactions.
MINTi MINT-2789553.
STRINGi 9606.ENSP00000361310.

Chemistry

BindingDBi Q9Y253.
ChEMBLi CHEMBL5542.

PTM databases

PhosphoSitei Q9Y253.

Polymorphism databases

DMDMi 59798441.

Proteomic databases

MaxQBi Q9Y253.
PaxDbi Q9Y253.
PRIDEi Q9Y253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372226 ; ENSP00000361300 ; ENSG00000170734 . [Q9Y253-2 ]
ENST00000372236 ; ENSP00000361310 ; ENSG00000170734 . [Q9Y253-1 ]
GeneIDi 5429.
KEGGi hsa:5429.
UCSCi uc003ovq.4. human. [Q9Y253-1 ]

Organism-specific databases

CTDi 5429.
GeneCardsi GC06P043543.
GeneReviewsi POLH.
HGNCi HGNC:9181. POLH.
HPAi HPA006721.
HPA026762.
MIMi 278750. phenotype.
603968. gene.
neXtProti NX_Q9Y253.
Orphaneti 90342. Xeroderma pigmentosum variant.
PharmGKBi PA279.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0389.
GeneTreei ENSGT00530000062942.
HOGENOMi HOG000115605.
HOVERGENi HBG053633.
InParanoidi Q9Y253.
KOi K03509.
OMAi SPPLTML.
PhylomeDBi Q9Y253.
TreeFami TF103010.

Enzyme and pathway databases

SABIO-RK Q9Y253.

Miscellaneous databases

EvolutionaryTracei Q9Y253.
GeneWikii DNA_polymerase_eta.
GenomeRNAii 5429.
NextBioi 21005.
PROi Q9Y253.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y253.
CleanExi HS_POLH.
ExpressionAtlasi Q9Y253. baseline and differential.
Genevestigatori Q9Y253.

Family and domain databases

Gene3Di 3.30.1490.100. 1 hit.
InterProi IPR017061. DNA_pol_eta.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
[Graphical view ]
Pfami PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF036603. DPol_eta. 1 hit.
SUPFAMi SSF100879. SSF100879. 1 hit.
PROSITEi PS50173. UMUC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The XPV (Xeroderma pigmentosum variant) gene encodes human DNA polymerase eta."
    Masutani C., Kusumoto R., Yamada A., Dohmae N., Yokoi M., Yuasa M., Araki M., Iwai S., Takio K., Hanaoka F.
    Nature 399:700-704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 132-163; 395-404; 429-450 AND 495-511, FUNCTION, INVOLVEMENT IN XPV, ALTERNATIVE SPLICING.
    Tissue: Cervix carcinoma.
  2. "hRAD30 mutations in the variant form of xeroderma pigmentosum."
    Johnson R.E., Kondratick C.M., Prakash S., Prakash L.
    Science 285:263-265(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT XPV LEU-75 DEL.
  3. "Genomic structure, chromosomal localization and identification of mutations in the xeroderma pigmentosum variant (XPV) gene."
    Yuasa M., Masutani C., Eki T., Hanaoka F.
    Oncogene 19:4721-4728(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN XPV.
  4. NIEHS SNPs program
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-209; TRP-334; MET-478; PRO-584; VAL-595 AND LEU-647.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 2).
    Tissue: Skin.
  7. "Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions."
    Glick E., Vigna K.L., Loeb L.A.
    EMBO J. 20:7303-7312(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS.
  8. "DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes."
    Zeng X., Winter D.B., Kasmer C., Kraemer K.H., Lehmann A.R., Gearhart P.J.
    Nat. Immunol. 2:537-541(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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 POLI.
  10. "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.
  11. "Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta."
    Glick E., Chau J.S., Vigna K.L., McCulloch S.D., Adman E.T., Kunkel T.A., Loeb L.A.
    J. Biol. Chem. 278:19341-19346(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-52.
  12. "DNA polymerase eta is involved in hypermutation occurring during immunoglobulin class switch recombination."
    Faili A., Aoufouchi S., Weller S., Vuillier F., Stary A., Sarasin A., Reynaud C.-A., Weill J.-C.
    J. Exp. Med. 199:265-270(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage."
    Kannouche P.L., Wing J., Lehmann A.R.
    Mol. Cell 14:491-500(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MONOUBIQUITINATED PCNA.
  14. "Regulation of translesion synthesis DNA polymerase eta by monoubiquitination."
    Bienko M., Green C.M., Sabbioneda S., Crosetto N., Matic I., Hibbert R.G., Begovic T., Niimi A., Mann M., Lehmann A.R., Dikic I.
    Mol. Cell 37:396-407(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-682; LYS-686; LYS-694 AND LYS-709.
  15. "Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis."
    Jung Y.S., Hakem A., Hakem R., Chen X.
    Mol. Cell. Biol. 31:3997-4006(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RCHY1/PIRH2.
  16. "Breast cancer proteins PALB2 and BRCA2 stimulate polymerase eta in recombination-associated DNA synthesis at blocked replication forks."
    Buisson R., Niraj J., Pauty J., Maity R., Zhao W., Coulombe Y., Sung P., Masson J.Y.
    Cell Rep. 6:553-564(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PALB2 AND BRCA2.
  17. "Xeroderma pigmentosum variant heterozygotes show reduced levels of recovery of replicative DNA synthesis in the presence of caffeine after ultraviolet irradiation."
    Itoh T., Linn S., Kamide R., Tokushige H., Katori N., Hosaka Y., Yamaizumi M.
    J. Invest. Dermatol. 115:981-985(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XPV GLU-535 AND THR-589.
  18. Cited for: VARIANTS XPV LEU-75 DEL; HIS-111 PRO-122; VAL-263 AND SER-361.
  19. "Correlation of phenotype/genotype in a cohort of 23 xeroderma pigmentosum-variant patients reveals 12 new disease-causing POLH mutations."
    Opletalova K., Bourillon A., Yang W., Pouvelle C., Armier J., Despras E., Ludovic M., Mateus C., Robert C., Kannouche P., Soufir N., Sarasin A.
    Hum. Mutat. 35:117-128(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XPV VAL-37 DEL; PRO-93; ASP-266; ARG-295 AND ALA-692.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-153.

Entry informationi

Entry nameiPOLH_HUMAN
AccessioniPrimary (citable) accession number: Q9Y253
Secondary accession number(s): Q7L8E3, Q96BC4, Q9BX13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 125 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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