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Q9Y253 (POLH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.9 Ref.13 Ref.16

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.17 Ref.18 Ref.19

Sequence similarities

Belongs to the DNA polymerase type-Y family.

Contains 1 umuC domain.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 713713DNA polymerase eta
PRO_0000173986

Regions

Domain9 – 259251UmuC

Sites

Metal binding131Magnesium By similarity
Metal binding1151Magnesium By similarity

Amino acid modifications

Cross-link682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Cross-link686Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Cross-link694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Cross-link709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Alternative sequence415 – 713299Missing in isoform 2.
VSP_012799
Natural variant371Missing in XPV. Ref.19
VAR_070835
Natural variant751Missing in XPV; impairs translesion synthesis. Ref.2 Ref.18
VAR_021226
Natural variant931R → P in XPV. Ref.19
VAR_070836
Natural variant1111R → H in XPV. Ref.18
VAR_021227
Natural variant1221T → P in XPV. Ref.18
VAR_021228
Natural variant1531G → D in a breast cancer sample; somatic mutation. Ref.20
VAR_036220
Natural variant2091G → V. Ref.4
Corresponds to variant rs2307456 [ dbSNP | Ensembl ].
VAR_021229
Natural variant2631G → V in XPV; impairs translesion synthesis. Ref.18
VAR_021230
Natural variant2661V → D in XPV. Ref.19
VAR_070837
Natural variant2951G → R in XPV. Ref.19
VAR_070838
Natural variant3341R → W. Ref.4
Corresponds to variant rs9333548 [ dbSNP | Ensembl ].
VAR_021231
Natural variant3611R → S in XPV. Ref.18
VAR_021232
Natural variant4781T → M. Ref.4
Corresponds to variant rs9296419 [ dbSNP | Ensembl ].
VAR_021233
Natural variant5351K → E in XPV. Ref.17
Corresponds to variant rs56307355 [ dbSNP | Ensembl ].
VAR_021234
Natural variant5841L → P. Ref.4
Corresponds to variant rs9333554 [ dbSNP | Ensembl ].
VAR_021235
Natural variant5891K → T in XPV. Ref.17
VAR_021236
Natural variant5951M → V. Ref.4
Corresponds to variant rs9333555 [ dbSNP | Ensembl ].
VAR_021237
Natural variant6471M → L. Ref.4
Corresponds to variant rs6941583 [ dbSNP | Ensembl ].
VAR_021238
Natural variant6921T → A in XPV. Ref.19
VAR_070839

Experimental info

Mutagenesis521Y → A or F: Reduces DNA polymerase activity. Ref.11
Mutagenesis521Y → E: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass. Ref.11

Secondary structure

............................................................................................. 713
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6D1D35A0F56ECE89

FASTA71378,413
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9ABB24D0511A45EB
Show »

FASTA41446,283

References

« Hide '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. expand/collapse author list , 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. 0:0-0(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]"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.
[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]"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. expand/collapse author list , 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.

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.
RefSeqNP_006493.1. NM_006502.2.
UniGeneHs.655467.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9Y253.
SMRQ9Y253. Positions 1-432, 629-662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111425. 18 interactions.
IntActQ9Y253. 5 interactions.
MINTMINT-2789553.
STRING9606.ENSP00000361310.

Chemistry

BindingDBQ9Y253.
ChEMBLCHEMBL5542.

PTM databases

PhosphoSiteQ9Y253.

Polymorphism databases

DMDM59798441.

Proteomic databases

PaxDbQ9Y253.
PRIDEQ9Y253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372226; ENSP00000361300; ENSG00000170734. [Q9Y253-2]
ENST00000372236; ENSP00000361310; ENSG00000170734. [Q9Y253-1]
GeneID5429.
KEGGhsa:5429.
UCSCuc003ovq.4. human. [Q9Y253-1]

Organism-specific databases

CTD5429.
GeneCardsGC06P043543.
HGNCHGNC:9181. POLH.
HPAHPA006721.
HPA026762.
MIM278750. phenotype.
603968. gene.
neXtProtNX_Q9Y253.
Orphanet90342. Xeroderma pigmentosum variant.
PharmGKBPA279.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0389.
HOGENOMHOG000115605.
HOVERGENHBG053633.
InParanoidQ9Y253.
KOK03509.
OMASPPLTML.
PhylomeDBQ9Y253.
TreeFamTF103010.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SABIO-RKQ9Y253.

Gene expression databases

ArrayExpressQ9Y253.
BgeeQ9Y253.
CleanExHS_POLH.
GenevestigatorQ9Y253.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
InterProIPR017061. 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]
PfamPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036603. DPol_eta. 1 hit.
SUPFAMSSF100879. SSF100879. 1 hit.
PROSITEPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y253.
GeneWikiDNA_polymerase_eta.
GenomeRNAi5429.
NextBio21005.
PROQ9Y253.
SOURCESearch...

Entry information

Entry namePOLH_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM