Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P18074

- ERCC2_HUMAN

UniProt

P18074 - ERCC2_HUMAN

Protein

TFIIH basal transcription factor complex helicase XPD subunit

Gene

ERCC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    ATP-dependent 5'-3' DNA helicase, component of the core-TFIIH basal transcription factor. Involved in nucleotide excision repair (NER) of DNA by opening DNA around the damage, and in RNA transcription by RNA polymerase II by anchoring the CDK-activating kinase (CAK) complex, composed of CDK7, cyclin H and MAT1, to the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Magnesium.1 Publication
    Binds 1 4Fe-4S cluster.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi116 – 1161Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi134 – 1341Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi155 – 1551Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi190 – 1901Iron-sulfur (4Fe-4S)Curated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 498ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. 5'-3' DNA helicase activity Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. ATP-dependent DNA helicase activity Source: InterPro
    5. DNA binding Source: UniProtKB-KW
    6. DNA-dependent ATPase activity Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: UniProtKB
    9. protein C-terminus binding Source: UniProtKB
    10. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. aging Source: Ensembl
    3. apoptotic process Source: UniProtKB
    4. ATP catabolic process Source: GOC
    5. bone mineralization Source: Ensembl
    6. cell proliferation Source: Ensembl
    7. central nervous system myelin formation Source: Ensembl
    8. chromosome segregation Source: UniProtKB
    9. DNA duplex unwinding Source: GOC
    10. DNA repair Source: Reactome
    11. embryonic cleavage Source: Ensembl
    12. erythrocyte maturation Source: Ensembl
    13. extracellular matrix organization Source: Ensembl
    14. gene expression Source: Reactome
    15. hair cell differentiation Source: UniProtKB
    16. hair follicle maturation Source: Ensembl
    17. hematopoietic stem cell differentiation Source: Ensembl
    18. in utero embryonic development Source: Ensembl
    19. multicellular organism growth Source: Ensembl
    20. nucleotide-excision repair Source: UniProtKB
    21. nucleotide-excision repair, DNA damage removal Source: Reactome
    22. nucleotide-excision repair, DNA incision Source: UniProtKB
    23. positive regulation of DNA binding Source: Ensembl
    24. positive regulation of transcription, DNA-templated Source: UniProtKB
    25. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    26. positive regulation of viral transcription Source: Reactome
    27. post-embryonic development Source: Ensembl
    28. protein phosphorylation Source: GOC
    29. regulation of mitotic cell cycle phase transition Source: UniProtKB
    30. response to hypoxia Source: Ensembl
    31. response to oxidative stress Source: UniProtKB
    32. small molecule metabolic process Source: Reactome
    33. spinal cord development Source: Ensembl
    34. termination of RNA polymerase I transcription Source: Reactome
    35. transcription-coupled nucleotide-excision repair Source: UniProtKB
    36. transcription elongation from RNA polymerase II promoter Source: Reactome
    37. transcription elongation from RNA polymerase I promoter Source: Reactome
    38. transcription from RNA polymerase II promoter Source: UniProtKB
    39. transcription from RNA polymerase I promoter Source: Reactome
    40. transcription initiation from RNA polymerase II promoter Source: Reactome
    41. transcription initiation from RNA polymerase I promoter Source: Reactome
    42. UV protection Source: MGI
    43. viral process Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Chromosome partition, DNA damage, DNA repair, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TFIIH basal transcription factor complex helicase XPD subunit (EC:3.6.4.12)
    Alternative name(s):
    Basic transcription factor 2 80 kDa subunit
    Short name:
    BTF2 p80
    CXPD
    DNA excision repair protein ERCC-2
    DNA repair protein complementing XP-D cells
    TFIIH basal transcription factor complex 80 kDa subunit
    Short name:
    TFIIH 80 kDa subunit
    Short name:
    TFIIH p80
    Xeroderma pigmentosum group D-complementing protein
    Gene namesi
    Name:ERCC2
    Synonyms:XPD, XPDC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3434. ERCC2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. holo TFIIH complex Source: UniProtKB
    3. MMXD complex Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Xeroderma pigmentosum complementation group D (XP-D) [MIM:278730]: 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. The skin develops marked freckling and other pigmentation abnormalities. Some XP-D patients present features of Cockayne syndrome, including cachectic dwarfism, pigmentary retinopathy, ataxia, decreased nerve conduction velocities. The phenotype combining xeroderma pigmentosum and Cockayne syndrome traits is referred to as XP-CS complex.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471G → R in XP-D.
    VAR_008187
    Natural varianti76 – 761T → A in XP-D.
    VAR_017282
    Natural varianti112 – 1121R → H in TTDP and XP-D. 3 Publications
    VAR_003622
    Natural varianti234 – 2341D → N in XP-D.
    VAR_008188
    Natural varianti461 – 4611L → V in XP-D and TTDP. 3 Publications
    VAR_003623
    Natural varianti485 – 4851L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 Publication
    VAR_017283
    Natural varianti511 – 5111R → Q in XP-D.
    VAR_017285
    Natural varianti541 – 5411S → R in XP-D; mild. 1 Publication
    Corresponds to variant rs121913019 [ dbSNP | Ensembl ].
    VAR_003625
    Natural varianti542 – 5421Y → C in XP-D.
    VAR_008191
    Natural varianti582 – 5832EK → VSE in XP-D.
    VAR_017286
    Natural varianti601 – 6011R → L in XP-D.
    VAR_008192
    Natural varianti601 – 6011R → W in XP-D.
    VAR_017289
    Natural varianti602 – 6021G → D in XP-D; combined with features of Cockayne syndrome.
    VAR_003627
    Natural varianti616 – 6161R → P in XP-D and TTDP. 1 Publication
    VAR_003626
    Natural varianti616 – 6161R → W in XP-D and COFS2. 1 Publication
    VAR_008193
    Natural varianti666 – 6661R → W in XP-D.
    VAR_017292
    Natural varianti675 – 6751G → R in XP-D/CS; severe form. 1 Publication
    VAR_003628
    Natural varianti681 – 6811D → N in XP-D and COFS2. 1 Publication
    VAR_017293
    Natural varianti683 – 6831R → Q in XP-D; CNS.
    VAR_008197
    Natural varianti683 – 6831R → W in XP-D; CNS; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter.
    Corresponds to variant rs41556519 [ dbSNP | Ensembl ].
    VAR_008198
    Natural varianti716 – 73015Missing in XP-D and TTDP.
    VAR_003629Add
    BLAST
    Trichothiodystrophy photosensitive (TTDP) [MIM:601675]: TTDP is an autosomal recessive disease characterized by sulfur-deficient brittle hair and nails, ichthyosis, mental retardation, impaired sexual development, abnormal facies and cutaneous photosensitivity correlated with a nucleotide excision repair (NER) defect. Neonates with trichothiodystrophy and ichthyosis are usually born with a collodion membrane. The severity of the ichthyosis after the membrane is shed is variable, ranging from a mild to severe lamellar ichthyotic phenotype. There are no reports of skin cancer associated with TTDP.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121R → H in TTDP and XP-D. 3 Publications
    VAR_003622
    Natural varianti259 – 2591C → Y in TTDP. 1 Publication
    VAR_008189
    Natural varianti461 – 4611L → V in XP-D and TTDP. 3 Publications
    VAR_003623
    Natural varianti482 – 4821Missing in TTDP. 1 Publication
    VAR_008190
    Natural varianti487 – 4871R → G in TTDP.
    VAR_017284
    Natural varianti488 – 4936Missing in TTDP; mild.
    VAR_003624
    Natural varianti592 – 5921R → P in TTDP.
    VAR_017287
    Natural varianti594 – 5941A → P in TTDP.
    VAR_017288
    Natural varianti616 – 6161R → P in XP-D and TTDP. 1 Publication
    VAR_003626
    Natural varianti658 – 6581R → C in TTDP. 2 Publications
    VAR_008194
    Natural varianti658 – 6581R → G in TTDP.
    VAR_017290
    Natural varianti658 – 6581R → H in TTDP.
    VAR_008195
    Natural varianti663 – 6631C → R in TTDP.
    VAR_017291
    Natural varianti673 – 6731D → G in TTDP. 1 Publication
    VAR_008196
    Natural varianti713 – 7131G → R in TTDP. 2 Publications
    VAR_008199
    Natural varianti716 – 73015Missing in XP-D and TTDP.
    VAR_003629Add
    BLAST
    Natural varianti722 – 7221R → W in TTDP. 2 Publications
    VAR_003630
    Natural varianti725 – 7251A → P in TTDP. 1 Publication
    VAR_003631
    Cerebro-oculo-facio-skeletal syndrome 2 (COFS2) [MIM:610756]: A disorder of prenatal onset characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. COFS is considered to be part of the nucleotide-excision repair disorders spectrum that include also xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti616 – 6161R → W in XP-D and COFS2. 1 Publication
    VAR_008193
    Natural varianti681 – 6811D → N in XP-D and COFS2. 1 Publication
    VAR_017293

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481K → R: Decreased transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi190 – 1901C → S: Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19. 1 Publication

    Keywords - Diseasei

    Cataract, Cockayne syndrome, Deafness, Disease mutation, Dwarfism, Ichthyosis, Xeroderma pigmentosum

    Organism-specific databases

    MIMi278730. phenotype.
    601675. phenotype.
    610756. phenotype.
    Orphaneti1466. COFS syndrome.
    33364. Trichothiodystrophy.
    276258. Xeroderma pigmentosum complementation group D.
    PharmGKBiPA27848.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760TFIIH basal transcription factor complex helicase XPD subunitPRO_0000101980Add
    BLAST

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP18074.
    PaxDbiP18074.
    PRIDEiP18074.

    PTM databases

    PhosphoSiteiP18074.

    Expressioni

    Gene expression databases

    ArrayExpressiP18074.
    BgeeiP18074.
    CleanExiHS_ERCC2.
    GenevestigatoriP18074.

    Organism-specific databases

    HPAiCAB005375.
    HPA038057.

    Interactioni

    Subunit structurei

    One of the six subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. The interaction with GTF2H2 results in the stimulation of the 5'-->3' helicase activity. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with FAM196B; the interaction is direct. Interacts with ATF7IP. Interacts with Epstein-Barr virus EBNA2.5 Publications

    Protein-protein interaction databases

    BioGridi108380. 24 interactions.
    DIPiDIP-644N.
    IntActiP18074. 10 interactions.
    MINTiMINT-3008891.
    STRINGi9606.ENSP00000375809.

    Structurei

    3D structure databases

    ProteinModelPortaliP18074.
    SMRiP18074. Positions 35-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 283277Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni438 – 637200Mediates interaction with MMS19Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi234 – 2374DEAH box
    Motifi682 – 69514Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the helicase family. RAD3/XPD subfamily.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1199.
    HOGENOMiHOG000205390.
    HOVERGENiHBG051498.
    InParanoidiP18074.
    KOiK10844.
    OMAiDEVWKYK.
    OrthoDBiEOG70W3CM.
    PhylomeDBiP18074.
    TreeFamiTF101232.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR006555. ATP-dep_Helicase_C.
    IPR010614. DEAD_2.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR013020. DNA_helicase_DNA-repair_Rad3.
    IPR010643. DUF1227.
    IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
    IPR006554. Helicase-like_DEXD_c2.
    IPR027417. P-loop_NTPase.
    IPR001945. XPGD_DNA_repair.
    [Graphical view]
    PfamiPF06733. DEAD_2. 1 hit.
    PF06777. DUF1227. 1 hit.
    PF13307. Helicase_C_2. 1 hit.
    [Graphical view]
    PRINTSiPR00852. XRODRMPGMNTD.
    SMARTiSM00488. DEXDc2. 1 hit.
    SM00491. HELICc2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    TIGRFAMsiTIGR00604. rad3. 1 hit.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51193. HELICASE_ATP_BIND_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18074-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV    50
    SLLALIMAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE 100
    KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT 150
    SLPHCRFYEE FDAHGREVPL PAGIYNLDDL KALGRRQGWC PYFLARYSIL 200
    HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN 250
    LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE 300
    TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV 350
    QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL 400
    ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PILHFSCMDA SLAIKPVFER 450
    FQSVIITSGT LSPLDIYPKI LDFHPVTMAT FTMTLARVCL CPMIIGRGND 500
    QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT SYQYMESTVA 550
    SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA 600
    RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND 650
    FLTFDAMRHA AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH 700
    LTDANLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLESEETL 750
    KRIEQIAQQL 760
    Length:760
    Mass (Da):86,909
    Last modified:November 1, 1990 - v1
    Checksum:i746C0888CDF2E331
    GO
    Isoform 2 (identifier: P18074-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: Missing.
         414-429: FTIIIEPFDDRTPTIA → QAQHCGSSRNQKRSHP
         430-760: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:405
    Mass (Da):46,274
    Checksum:iD56A486AC3C9D222
    GO

    Sequence cautioni

    The sequence AAM45142.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471G → R in XP-D.
    VAR_008187
    Natural varianti76 – 761T → A in XP-D.
    VAR_017282
    Natural varianti112 – 1121R → H in TTDP and XP-D. 3 Publications
    VAR_003622
    Natural varianti199 – 1991I → M.
    Corresponds to variant rs1799791 [ dbSNP | Ensembl ].
    VAR_011412
    Natural varianti201 – 2011H → Y.
    Corresponds to variant rs1799792 [ dbSNP | Ensembl ].
    VAR_011413
    Natural varianti234 – 2341D → N in XP-D.
    VAR_008188
    Natural varianti259 – 2591C → Y in TTDP. 1 Publication
    VAR_008189
    Natural varianti312 – 3121D → N.4 Publications
    Corresponds to variant rs1799793 [ dbSNP | Ensembl ].
    VAR_011414
    Natural varianti461 – 4611L → V in XP-D and TTDP. 3 Publications
    VAR_003623
    Natural varianti482 – 4821Missing in TTDP. 1 Publication
    VAR_008190
    Natural varianti485 – 4851L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 Publication
    VAR_017283
    Natural varianti487 – 4871R → G in TTDP.
    VAR_017284
    Natural varianti488 – 4936Missing in TTDP; mild.
    VAR_003624
    Natural varianti511 – 5111R → Q in XP-D.
    VAR_017285
    Natural varianti541 – 5411S → R in XP-D; mild. 1 Publication
    Corresponds to variant rs121913019 [ dbSNP | Ensembl ].
    VAR_003625
    Natural varianti542 – 5421Y → C in XP-D.
    VAR_008191
    Natural varianti582 – 5832EK → VSE in XP-D.
    VAR_017286
    Natural varianti592 – 5921R → P in TTDP.
    VAR_017287
    Natural varianti594 – 5941A → P in TTDP.
    VAR_017288
    Natural varianti601 – 6011R → L in XP-D.
    VAR_008192
    Natural varianti601 – 6011R → W in XP-D.
    VAR_017289
    Natural varianti602 – 6021G → D in XP-D; combined with features of Cockayne syndrome.
    VAR_003627
    Natural varianti616 – 6161R → C.1 Publication
    VAR_011415
    Natural varianti616 – 6161R → P in XP-D and TTDP. 1 Publication
    VAR_003626
    Natural varianti616 – 6161R → W in XP-D and COFS2. 1 Publication
    VAR_008193
    Natural varianti658 – 6581R → C in TTDP. 2 Publications
    VAR_008194
    Natural varianti658 – 6581R → G in TTDP.
    VAR_017290
    Natural varianti658 – 6581R → H in TTDP.
    VAR_008195
    Natural varianti663 – 6631C → R in TTDP.
    VAR_017291
    Natural varianti666 – 6661R → W in XP-D.
    VAR_017292
    Natural varianti673 – 6731D → G in TTDP. 1 Publication
    VAR_008196
    Natural varianti675 – 6751G → R in XP-D/CS; severe form. 1 Publication
    VAR_003628
    Natural varianti681 – 6811D → N in XP-D and COFS2. 1 Publication
    VAR_017293
    Natural varianti683 – 6831R → Q in XP-D; CNS.
    VAR_008197
    Natural varianti683 – 6831R → W in XP-D; CNS; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter.
    Corresponds to variant rs41556519 [ dbSNP | Ensembl ].
    VAR_008198
    Natural varianti713 – 7131G → R in TTDP. 2 Publications
    VAR_008199
    Natural varianti716 – 73015Missing in XP-D and TTDP.
    VAR_003629Add
    BLAST
    Natural varianti722 – 7221R → W in TTDP. 2 Publications
    VAR_003630
    Natural varianti725 – 7251A → P in TTDP. 1 Publication
    VAR_003631
    Natural varianti751 – 7511K → Q May be linked to a reduced activity. 6 Publications
    Corresponds to variant rs13181 [ dbSNP | Ensembl ].
    VAR_011416

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2424Missing in isoform 2. 1 PublicationVSP_043132Add
    BLAST
    Alternative sequencei414 – 42916FTIII…TPTIA → QAQHCGSSRNQKRSHP in isoform 2. 1 PublicationVSP_043133Add
    BLAST
    Alternative sequencei430 – 760331Missing in isoform 2. 1 PublicationVSP_043134Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52221 mRNA. Translation: CAA36463.1.
    X52222 mRNA. Translation: CAA36464.1.
    L47234 Genomic DNA. Translation: AAL48323.1.
    AY092780 Genomic DNA. Translation: AAM45142.1. Sequence problems.
    BT006883 mRNA. Translation: AAP35529.1.
    CH471126 Genomic DNA. Translation: EAW57341.1.
    BC108255 mRNA. Translation: AAI08256.1.
    BC110523 mRNA. Translation: AAI10524.1.
    CCDSiCCDS33049.1. [P18074-1]
    CCDS46112.1. [P18074-2]
    PIRiS10888.
    RefSeqiNP_000391.1. NM_000400.3. [P18074-1]
    NP_001124339.1. NM_001130867.1. [P18074-2]
    XP_005258696.1. XM_005258639.1.
    UniGeneiHs.487294.

    Genome annotation databases

    EnsembliENST00000391945; ENSP00000375809; ENSG00000104884. [P18074-1]
    ENST00000485403; ENSP00000431229; ENSG00000104884. [P18074-2]
    GeneIDi2068.
    KEGGihsa:2068.
    UCSCiuc002pbj.2. human. [P18074-1]
    uc002pbl.4. human. [P18074-2]

    Polymorphism databases

    DMDMi119540.

    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
    X52221 mRNA. Translation: CAA36463.1 .
    X52222 mRNA. Translation: CAA36464.1 .
    L47234 Genomic DNA. Translation: AAL48323.1 .
    AY092780 Genomic DNA. Translation: AAM45142.1 . Sequence problems.
    BT006883 mRNA. Translation: AAP35529.1 .
    CH471126 Genomic DNA. Translation: EAW57341.1 .
    BC108255 mRNA. Translation: AAI08256.1 .
    BC110523 mRNA. Translation: AAI10524.1 .
    CCDSi CCDS33049.1. [P18074-1 ]
    CCDS46112.1. [P18074-2 ]
    PIRi S10888.
    RefSeqi NP_000391.1. NM_000400.3. [P18074-1 ]
    NP_001124339.1. NM_001130867.1. [P18074-2 ]
    XP_005258696.1. XM_005258639.1.
    UniGenei Hs.487294.

    3D structure databases

    ProteinModelPortali P18074.
    SMRi P18074. Positions 35-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108380. 24 interactions.
    DIPi DIP-644N.
    IntActi P18074. 10 interactions.
    MINTi MINT-3008891.
    STRINGi 9606.ENSP00000375809.

    PTM databases

    PhosphoSitei P18074.

    Polymorphism databases

    DMDMi 119540.

    Proteomic databases

    MaxQBi P18074.
    PaxDbi P18074.
    PRIDEi P18074.

    Protocols and materials databases

    DNASUi 2068.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000391945 ; ENSP00000375809 ; ENSG00000104884 . [P18074-1 ]
    ENST00000485403 ; ENSP00000431229 ; ENSG00000104884 . [P18074-2 ]
    GeneIDi 2068.
    KEGGi hsa:2068.
    UCSCi uc002pbj.2. human. [P18074-1 ]
    uc002pbl.4. human. [P18074-2 ]

    Organism-specific databases

    CTDi 2068.
    GeneCardsi GC19M045854.
    GeneReviewsi ERCC2.
    HGNCi HGNC:3434. ERCC2.
    HPAi CAB005375.
    HPA038057.
    MIMi 126340. gene.
    278730. phenotype.
    601675. phenotype.
    610756. phenotype.
    neXtProti NX_P18074.
    Orphaneti 1466. COFS syndrome.
    33364. Trichothiodystrophy.
    276258. Xeroderma pigmentosum complementation group D.
    PharmGKBi PA27848.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1199.
    HOGENOMi HOG000205390.
    HOVERGENi HBG051498.
    InParanoidi P18074.
    KOi K10844.
    OMAi DEVWKYK.
    OrthoDBi EOG70W3CM.
    PhylomeDBi P18074.
    TreeFami TF101232.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    ChiTaRSi ERCC2. human.
    GeneWikii ERCC2.
    GenomeRNAii 2068.
    NextBioi 8409.
    PROi P18074.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18074.
    Bgeei P18074.
    CleanExi HS_ERCC2.
    Genevestigatori P18074.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR006555. ATP-dep_Helicase_C.
    IPR010614. DEAD_2.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR013020. DNA_helicase_DNA-repair_Rad3.
    IPR010643. DUF1227.
    IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
    IPR006554. Helicase-like_DEXD_c2.
    IPR027417. P-loop_NTPase.
    IPR001945. XPGD_DNA_repair.
    [Graphical view ]
    Pfami PF06733. DEAD_2. 1 hit.
    PF06777. DUF1227. 1 hit.
    PF13307. Helicase_C_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00852. XRODRMPGMNTD.
    SMARTi SM00488. DEXDc2. 1 hit.
    SM00491. HELICc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    TIGRFAMsi TIGR00604. rad3. 1 hit.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51193. HELICASE_ATP_BIND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERCC2: cDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3."
      Weber C.A., Salazar E.P., Stewart S.A., Thompson L.H.
      EMBO J. 9:1437-1447(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    2. "Sequence analysis of the ERCC2 gene regions in human, mouse, and hamster reveals three linked genes."
      Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.
      Genomics 34:399-409(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Fibroblast.
    3. NIEHS SNPs program
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-312 AND GLN-751.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-751.
    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 1), VARIANT GLN-751.
      Tissue: Testis.
    7. "Correction of Xeroderma pigmentosum complementation group D mutant cell phenotypes by chromosome and gene transfer: involvement of the human ERCC2 DNA repair gene."
      Fletjer W.L., McDaniel L.D., Johns D., Friedberg E.C., Schultz R.A.
      Proc. Natl. Acad. Sci. U.S.A. 89:261-265(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Human Xeroderma pigmentosum group D gene encodes a DNA helicase."
      Sung P., Bailly V., Weber C.A., Thompson L.H., Prakash L., Prakash S.
      Nature 365:852-855(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2."
      Tong X., Drapkin R., Reinberg D., Kieff E.
      Proc. Natl. Acad. Sci. U.S.A. 92:3259-3263(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV EBNA2.
    10. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
      Kershnar E., Wu S.-Y., Chiang C.-M.
      J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
    11. "Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH."
      Coin F., Marinoni J.-C., Rodolfo C., Fribourg S., Pedrini A.M., Egly J.-M.
      Nat. Genet. 20:184-188(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GTF2H2.
    12. "Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7."
      Tirode F., Busso D., Coin F., Egly J.-M.
      Mol. Cell 3:87-95(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-48, FUNCTION.
    13. "Selective regulation of vitamin D receptor-responsive genes by TFIIH."
      Drane P., Compe E., Catez P., Chymkowitch P., Egly J.-M.
      Mol. Cell 16:187-197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, POSSIBLE PATHOLOGICAL MECHANISM OF VARIANT XP-D TRP-683.
    14. "Identification and Herc5-mediated ISGylation of novel target proteins."
      Takeuchi T., Inoue S., Yokosawa H.
      Biochem. Biophys. Res. Commun. 348:473-477(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.
    15. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
      Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
      J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP.
    16. "MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation."
      Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., Kuraoka I., Hiraoka Y., Tanaka K.
      Mol. Cell 39:632-640(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN MMXD COMPLEX, INTERACTION WITH FAM196B, SUBCELLULAR LOCATION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism."
      Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.
      Science 337:243-245(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IRON-SULFUR-BINDING, COFACTOR, MUTAGENESIS OF CYS-190.
    19. "Structural and mutational analysis of the xeroderma pigmentosum group D (XPD) gene."
      Frederick G.D., Amirkhan R.H., Schultz R.A., Friedberg E.C.
      Hum. Mol. Genet. 3:1783-1788(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-D VAL-461.
    20. "Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy."
      Broughton B.C., Steingrimsdottir H., Weber C.A., Lehmann A.R.
      Nat. Genet. 7:189-194(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP HIS-112; PRO-616; TRP-722 AND 488-VAL--MET-493 DEL.
    21. "Molecular and cellular analysis of the DNA repair defect in a patient in xeroderma pigmentosum complementation group D who has the clinical features of xeroderma pigmentosum and Cockayne syndrome."
      Broughton B.C., Thompson A.F., Harcourt S.A., Vermeulen W., Hoeijmakers J.H.J., Botta E., Stefanini M., King M.D., Weber C.A., Cole J., Arlett C.F., Lehmann A.R.
      Am. J. Hum. Genet. 56:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-D ARG-675.
    22. "Defects in the DNA repair and transcription gene ERCC2 in the cancer-prone disorder xeroderma pigmentosum group D."
      Takayama K., Salazar E.P., Lehmann A.R., Stefanini M., Thompson L.H., Weber C.A.
      Cancer Res. 55:5656-5663(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XP-D.
    23. "Defects in the DNA repair and transcription gene ERCC2(XPD) in trichothiodystrophy."
      Takayama K., Salazar E.P., Broughton B.C., Lehmann A.R., Sarasin A., Thompson L.H., Weber C.A.
      Am. J. Hum. Genet. 58:263-270(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP CYS-658 AND ARG-713.
    24. "Mutations in the XPD gene leading to Xeroderma pigmentosum symptoms."
      Kobayashi T., Kuraoka I., Saijo M., Nakatsu Y., Tanaka A., Someda Y., Fukuro S., Tanaka K.
      Hum. Mutat. 9:322-331(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XP-D ARG-541.
    25. "DNA repair characteristics and mutations in the ERCC2 DNA repair and transcription gene in a trichothiodystrophy patient."
      Takayama K., Danks D.M., Salazar E.P., Cleaver J.E., Weber C.A.
      Hum. Mutat. 9:519-525(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP VAL-461; 716-VAL--ARG-730 DEL AND PRO-725.
    26. "Xeroderma pigmentosum and trichothiodystrophy are associated with different mutations in the XPD (ERCC2) repair/transcription gene."
      Taylor E.M., Broughton B.C., Botta E., Stefanini M., Sarasin A., Jaspers N.G.J., Fawcett H., Harcourt S.A., Arlett C.F., Lehmann A.R.
      Proc. Natl. Acad. Sci. U.S.A. 94:8658-8663(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP/XP.
    27. "Analysis of mutations in the XPD gene in Italian patients with trichothiodystrophy: site of mutation correlates with repair deficiency, but gene dosage appears to determine clinical severity."
      Botta E., Nardo T., Broughton B.C., Marinoni S., Lehmann A.R., Stefanini M.
      Am. J. Hum. Genet. 63:1036-1048(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP HIS-112; TYR-259; VAL-461; THR-482 DEL; GLY-673 AND TRP-722.
    28. "A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy."
      Cleaver J.E., Thompson L.H., Richardson A.S., States J.C.
      Hum. Mutat. 14:9-22(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS XP-D.
    29. "Cerebro-oculo-facio-skeletal syndrome with a nucleotide excision-repair defect and a mutated XPD gene, with prenatal diagnosis in a triplet pregnancy."
      Graham J.M. Jr., Anyane-Yeboa K., Raams A., Appeldoorn E., Kleijer W.J., Garritsen V.H., Busch D., Edersheim T.G., Jaspers N.G.J.
      Am. J. Hum. Genet. 69:291-300(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS COFS2 TRP-616 AND ASN-681.
    30. "Associations between ercc2 polymorphisms and gliomas."
      Caggana M., Kilgallen J., Conroy J.M., Wiencke J.K., Kelsey K.T., Miike R., Chen P., Wrensch M.R.
      Cancer Epidemiol. Biomarkers Prev. 10:355-360(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-616.
    31. "Modulation of nucleotide excision repair capacity by XPD polymorphisms in lung cancer patients."
      Spitz M.R., Wu X., Wang Y., Wang L.E., Shete S., Amos C.I., Guo Z., Lei L., Mohrenweiser H., Wei Q.
      Cancer Res. 61:1354-1357(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASN-312 AND GLN-751.
    32. "XPD exon 10 and 23 polymorphisms and DNA repair in human skin in situ."
      Hemminki K., Xu G., Angelini S., Snellman E., Jansen C.T., Lambert B., Hou S.M.
      Carcinogenesis 22:1185-1188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASN-312 AND GLN-751.
    33. "The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases."
      Lehmann A.R.
      Genes Dev. 15:15-23(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    34. "Two individuals with features of both xeroderma pigmentosum and trichothiodystrophy highlight the complexity of the clinical outcomes of mutations in the XPD gene."
      Broughton B.C., Berneburg M., Fawcett H., Taylor E.M., Arlett C.F., Nardo T., Stefanini M., Menefee E., Price V.H., Queille S., Sarasin A., Bohnert E., Krutmann J., Davidson R., Kraemer K.H., Lehmann A.R.
      Hum. Mol. Genet. 10:2539-2547(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XP-D HIS-112; PRO-485 AND 582-GLU-LYS-583 DELINS VAL-SER-GLU, VARIANTS ASN-312 AND GLN-751.
    35. "A temperature-sensitive disorder in basal transcription and DNA repair in humans."
      Vermeulen W., Rademakers S., Jaspers N.G.J., Appeldoorn E., Raams A., Klein B., Kleijer W.J., Hansen L.K., Hoeijmakers J.H.J.
      Nat. Genet. 27:299-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTDP CYS-658 AND ARG-713.

    Entry informationi

    Entry nameiERCC2_HUMAN
    AccessioniPrimary (citable) accession number: P18074
    Secondary accession number(s): Q2TB78
    , Q2YDY2, Q7KZU6, Q8N721
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 179 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3