Q9Y253 (POLH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase eta
EC=2.7.7.7

Alternative name(s):
RAD30 homolog A
Xeroderma pigmentosum variant type protein

Gene names

Name:	POLH
Synonyms:	RAD30, RAD30A, XPV

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	713 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7 Ref.8 Ref.10 Ref.12
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Divalent metal cations. Prefers magnesium, but can also use manganese.
Subunit structure	Interacts with REV1 By similarity. Interacts with monoubiquitinated PCNA, but not unmodified PCNA. Interacts with POLI. Ref.9 Ref.13
Subcellular location	Nucleus. Note: Accumulates at replication forks after DNA damage. Ref.9
Domain	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.
Post-translational modification	Monoubiquitinated by RCHY1/PIRH2; ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.3 Ref.16 Ref.17
Sequence similarities	Belongs to the DNA polymerase type-Y family. Contains 1 umuC domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication DNA synthesis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Xeroderma pigmentosum
Ligand	DNA-binding Magnesium Metal-binding Schiff base
Molecular function	DNA-directed DNA polymerase Mutator protein Nucleotidyltransferase Transferase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW DNA synthesis involved in DNA repair Inferred from direct assay PubMed 17563354. Source: UniProtKB postreplication repair Inferred from electronic annotation. Source: Compara pyrimidine dimer repair Inferred from electronic annotation. Source: Compara regulation of DNA repair Traceable author statement Ref.2. Source: ProtInc response to UV-C Inferred from direct assay PubMed 17563354. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA-directed DNA polymerase activity Traceable author statement. Source: Reactome damaged DNA binding Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y253-1)

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.

Isoform 2 (identifier: Q9Y253-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 713

713

DNA polymerase eta

PRO_0000173986

Regions

Domain

9 – 259

251

UmuC

Sites

Metal binding

13

1

Magnesium By similarity

Metal binding

115

1

Magnesium By similarity

Amino acid modifications

Cross-link

682

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Cross-link

686

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Cross-link

694

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Cross-link

709

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Alternative sequence

415 – 713

299

Missing in isoform 2.

VSP_012799

Natural variant

75

1

Missing in XPV; impairs translesion synthesis. Ref.2 Ref.17

VAR_021226

Natural variant

111

1

R → H in XPV. Ref.17

VAR_021227

Natural variant

122

1

T → P in XPV. Ref.17

VAR_021228

Natural variant

153

1

G → D in a breast cancer sample; somatic mutation. Ref.18

VAR_036220

Natural variant

209

1

G → V. Ref.4
Corresponds to variant rs2307456 [ dbSNP | Ensembl ].

VAR_021229

Natural variant

263

1

G → V in XPV; impairs translesion synthesis. Ref.17

VAR_021230

Natural variant

334

1

R → W. Ref.4
Corresponds to variant rs9333548 [ dbSNP | Ensembl ].

VAR_021231

Natural variant

361

1

R → S in XPV. Ref.17

VAR_021232

Natural variant

478

1

T → M. Ref.4
Corresponds to variant rs9296419 [ dbSNP | Ensembl ].

VAR_021233

Natural variant

535

1

K → E in XPV. Ref.16
Corresponds to variant rs56307355 [ dbSNP | Ensembl ].

VAR_021234

Natural variant

584

1

L → P. Ref.4
Corresponds to variant rs9333554 [ dbSNP | Ensembl ].

VAR_021235

Natural variant

589

1

K → T in XPV. Ref.16

VAR_021236

Natural variant

595

1

M → V. Ref.4
Corresponds to variant rs9333555 [ dbSNP | Ensembl ].

VAR_021237

Natural variant

647

1

M → L. Ref.4
Corresponds to variant rs6941583 [ dbSNP | Ensembl ].

VAR_021238

Experimental info

Mutagenesis

52

1

Y → A or F: Reduces DNA polymerase activity. Ref.11

Mutagenesis

52

1

Y → E: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass. Ref.11

Secondary structure

1

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713

Helix Strand Turn

Details...

Helix

1 – 3

3

Beta strand

9 – 14

6

Helix

17 – 25

9

Helix

27 – 29

3

Beta strand

34 – 38

5

Turn

41 – 44

4

Beta strand

46 – 50

5

Helix

52 – 55

4

Turn

56 – 58

3

Beta strand

61 – 64

4

Helix

65 – 71

7

Beta strand

76 – 79

4

Beta strand

81 – 83

3

Beta strand

86 – 88

3

Helix

90 – 106

17

Beta strand

109 – 113

5

Beta strand

116 – 120

5

Helix

122 – 132

11

Helix

139 – 141

3

Beta strand

145 – 147

3

Helix

159 – 161

3

Helix

163 – 177

15

Helix

186 – 208

23

Beta strand

212 – 219

8

Helix

220 – 229

10

Beta strand

235 – 237

3

Helix

240 – 242

3

Helix

243 – 248

6

Helix

252 – 254

3

Helix

261 – 270

10

Helix

275 – 280

6

Helix

283 – 290

8

Helix

292 – 301

10

Turn

302 – 304

3

Beta strand

313 – 315

3

Beta strand

319 – 324

6

Helix

327 – 329

3

Beta strand

331 – 333

3

Helix

334 – 359

26

Beta strand

360 – 372

13

Beta strand

376 – 378

3

Beta strand

380 – 386

7

Helix

392 – 403

12

Helix

404 – 406

3

Beta strand

414 – 431

18

Helix

532 – 538

7

Beta strand

632 – 634

3

Turn

636 – 638

3

Beta strand

641 – 643

3

Helix

644 – 646

3

Helix

647 – 659

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 6D1D35A0F56ECE89	FASTA	713	78,413
	10 20 30 40 50 60 MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV SYEARAFGVT 70 80 90 100 110 120 RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM EIMSRFAVIE RASIDEAYVD 130 140 150 160 170 180 LTSAVQERLQ KLQGQPISAD LLPSTYIEGL PQGPTTAEET VQKEGMRKQG LFQWLDSLQI 190 200 210 220 230 240 DNLTSPDLQL TVGAVIVEEM RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH 250 260 270 280 290 300 GSVPQLFSQM PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA 310 320 330 340 350 360 MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE RLTKDRNDND 370 380 390 400 410 420 RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF TVIKNCNTSG IQTEWSPPLT 430 440 450 460 470 480 MLFLCATKFS ASAPSSSTDI TSFLSSDPSS LPKVPVTSSE AKTQGSGPAV TATKKATTSL 490 500 510 520 530 540 ESFFQKAAER QKVKEASLSS LTAPTQAPMS NSPSKPSLPF QTSQSTGTEP FFKQKSLLLK 550 560 570 580 590 600 QKQLNNSSVS SPQQNPWSNC KALPNSLPTE YPGCVPVCEG VSKLEESSKA TPAEMDLAHN 610 620 630 640 650 660 SQSMHASSAS KSVLEVTQKA TPNPSLLAAE DQVPCEKCGS LVPVWDMPEH MDYHFALELQ 670 680 690 700 710 KSFLQPHSSN PQVVSAVSHQ GKRNPKSPLA CTNKRPRPEG MQTLESFFKP LTH
	Isoform 2 [UniParc]. Checksum: 9ABB24D0511A45EB	FASTA	414	46,283
	10 20 30 40 50 60 MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV SYEARAFGVT 70 80 90 100 110 120 RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM EIMSRFAVIE RASIDEAYVD 130 140 150 160 170 180 LTSAVQERLQ KLQGQPISAD LLPSTYIEGL PQGPTTAEET VQKEGMRKQG LFQWLDSLQI 190 200 210 220 230 240 DNLTSPDLQL TVGAVIVEEM RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH 250 260 270 280 290 300 GSVPQLFSQM PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA 310 320 330 340 350 360 MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE RLTKDRNDND 370 380 390 400 410 RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF TVIKNCNTSG IQTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[17]	"Molecular analysis of mutations in DNA polymerase eta in xeroderma pigmentosum variant patients." Broughton B.C., Cordonnier A., Kleijer W.J., Jaspers N.G., Fawcett H., Raams A., Garritsen V.H., Stary A., Avril M.-F., Boudsocq F., Masutani C., Hanaoka F., Fuchs R.P.P., Sarasin A., Lehmann A.R. Proc. Natl. Acad. Sci. U.S.A. 99:815-820(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS XPV LEU-75 DEL; HIS-111 PRO-122; VAL-263 AND SER-361.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-153.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00008011.
IPI00552037.

RefSeq

NP_006493.1. NM_006502.2.

UniGene

Hs.655467.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y253.

ModBase

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Protein-protein interaction databases

IntAct

Q9Y253. 1 interaction.

MINT

MINT-2789553.

STRING

9606.ENSP00000361310.

PTM databases

PhosphoSite

Q9Y253.

Polymorphism databases

DMDM

59798441.

Proteomic databases

PaxDb

Q9Y253.

PRIDE

Q9Y253.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372226; ENSP00000361300; ENSG00000170734.
ENST00000372236; ENSP00000361310; ENSG00000170734.

GeneID

5429.

KEGG

hsa:5429.

UCSC

uc003ovq.4. human.

Organism-specific databases

CTD

5429.

GeneCards

GC06P043543.

HGNC

HGNC:9181. POLH.

HPA

HPA006721.
HPA026762.

MIM

278750. phenotype.
603968. gene.

neXtProt

NX_Q9Y253.

Orphanet

90342. Xeroderma pigmentosum variant.

PharmGKB

PA279.

GenAtlas

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Phylogenomic databases

eggNOG

COG0389.

HOGENOM

HOG000115605.

HOVERGEN

HBG053633.

InParanoid

Q9Y253.

KO

K03509.

OMA

SPPLTML.

OrthoDB

EOG4RBQJ8.

PhylomeDB

Q9Y253.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

SABIO-RK

Q9Y253.

Gene expression databases

ArrayExpress

Q9Y253.

Bgee

Q9Y253.

CleanEx

HS_POLH.

Genevestigator

Q9Y253.

GermOnline

ENSG00000170734. Homo sapiens.

Family and domain databases

Gene3D

3.30.1490.100. 1 hit.

InterPro

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]

Pfam

PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]

PIRSF

PIRSF036603. DPol_eta. 1 hit.

SUPFAM

SSF100879. DNA_pol_Y-fam_little_finger. 1 hit.

PROSITE

PS50173. UMUC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y253.

ChEMBL

CHEMBL5542.

EvolutionaryTrace

Q9Y253.

GenomeRNAi

5429.

NextBio

21005.

SOURCE

Search...

Entry information

Entry name

POLH_HUMAN

Accession

Primary (citable) accession number: Q9Y253
Secondary accession number(s): Q7L8E3, Q96BC4, Q9BX13

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 109 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.