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Protein

TFIIH basal transcription factor complex helicase XPD subunit

Gene

ERCC2

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

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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi116Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi134Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi155Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi190Iron-sulfur (4Fe-4S)Curated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 49ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 5'-3' DNA helicase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: InterPro
  • DNA binding Source: UniProtKB-KW
  • DNA-dependent ATPase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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

BioCyciZFISH:ENSG00000104884-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-2564830. Cytosolic iron-sulfur cluster assembly.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiP18074.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3434. ERCC2.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: Ensembl
  • cytoplasm Source: UniProtKB
  • holo TFIIH complex Source: UniProtKB
  • MMXD complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
  • transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group D (XP-D)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:278730
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00818747G → R in XP-D. 1
Natural variantiVAR_01728276T → A in XP-D. 1
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant rs121913020dbSNPEnsembl.1
Natural variantiVAR_008188234D → N in XP-D. 1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant rs121913016dbSNPEnsembl.1
Natural variantiVAR_017283485L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 PublicationCorresponds to variant rs121913025dbSNPEnsembl.1
Natural variantiVAR_017285511R → Q in XP-D. Corresponds to variant rs772572683dbSNPEnsembl.1
Natural variantiVAR_003625541S → R in XP-D; mild. 1 PublicationCorresponds to variant rs121913019dbSNPEnsembl.1
Natural variantiVAR_008191542Y → C in XP-D. 1
Natural variantiVAR_017286582 – 583EK → VSE in XP-D. 1 Publication2
Natural variantiVAR_008192601R → L in XP-D. Corresponds to variant rs140522180dbSNPEnsembl.1
Natural variantiVAR_017289601R → W in XP-D. Corresponds to variant rs753641926dbSNPEnsembl.1
Natural variantiVAR_003627602G → D in XP-D; combined with features of Cockayne syndrome. Corresponds to variant rs771824813dbSNPEnsembl.1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant rs376556895dbSNPEnsembl.1
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913024dbSNPEnsembl.1
Natural variantiVAR_017292666R → W in XP-D. Corresponds to variant rs752510317dbSNPEnsembl.1
Natural variantiVAR_003628675G → R in XP-D/CS; severe form. 1 Publication1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913023dbSNPEnsembl.1
Natural variantiVAR_008197683R → Q in XP-D. 1
Natural variantiVAR_008198683R → W in XP-D; 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. 1 PublicationCorresponds to variant rs41556519dbSNPEnsembl.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Trichothiodystrophy 1, photosensitive (TTD1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of trichothiodystrophy, an autosomal recessive disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non-photosensitive forms of the disorder. TTD1 patients manifest cutaneous photosensitivity.
See also OMIM:601675
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant rs121913020dbSNPEnsembl.1
Natural variantiVAR_008189259C → Y in TTD1. 1 PublicationCorresponds to variant rs370454709dbSNPEnsembl.1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant rs121913016dbSNPEnsembl.1
Natural variantiVAR_008190482Missing in TTD1. 1 Publication1
Natural variantiVAR_017284487R → G in TTD1. 1
Natural variantiVAR_003624488 – 493Missing in TTD1; mild. 1 Publication6
Natural variantiVAR_017287592R → P in TTD1. 1
Natural variantiVAR_017288594A → P in TTD1. 1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant rs376556895dbSNPEnsembl.1
Natural variantiVAR_008194658R → C in TTD1. 2 PublicationsCorresponds to variant rs121913021dbSNPEnsembl.1
Natural variantiVAR_017290658R → G in TTD1. 1
Natural variantiVAR_008195658R → H in TTD1. Corresponds to variant rs762141272dbSNPEnsembl.1
Natural variantiVAR_017291663C → R in TTD1. Corresponds to variant rs770367713dbSNPEnsembl.1
Natural variantiVAR_008196673D → G in TTD1. 1 Publication1
Natural variantiVAR_008199713G → R in TTD1. 2 PublicationsCorresponds to variant rs121913022dbSNPEnsembl.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Natural variantiVAR_003630722R → W in TTD1. 2 PublicationsCorresponds to variant rs121913026dbSNPEnsembl.1
Natural variantiVAR_003631725A → P in TTD1. 1 PublicationCorresponds to variant rs121913018dbSNPEnsembl.1
Cerebro-oculo-facio-skeletal syndrome 2 (COFS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:610756
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913024dbSNPEnsembl.1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913023dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48K → R: Decreased transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi190C → S: Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19. 1 Publication1

Keywords - Diseasei

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

Organism-specific databases

DisGeNETi2068.
MalaCardsiERCC2.
MIMi278730. phenotype.
601675. phenotype.
610756. phenotype.
OpenTargetsiENSG00000104884.
Orphaneti1466. COFS syndrome.
33364. Trichothiodystrophy.
276258. Xeroderma pigmentosum complementation group D.
PharmGKBiPA27848.

Polymorphism and mutation databases

BioMutaiERCC2.
DMDMi119540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001019801 – 760TFIIH basal transcription factor complex helicase XPD subunitAdd BLAST760

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiP18074.
MaxQBiP18074.
PaxDbiP18074.
PeptideAtlasiP18074.
PRIDEiP18074.

PTM databases

iPTMnetiP18074.
PhosphoSitePlusiP18074.

Expressioni

Gene expression databases

BgeeiENSG00000104884.
CleanExiHS_ERCC2.
ExpressionAtlasiP18074. baseline and differential.
GenevisibleiP18074. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2H2C_2Q6P1K83EBI-6380590,EBI-8469755

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108380. 34 interactors.
DIPiDIP-644N.
IntActiP18074. 14 interactors.
MINTiMINT-3008891.
STRINGi9606.ENSP00000375809.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IVWelectron microscopy10.00W1-760[»]
5IY6electron microscopy7.20W1-760[»]
5IY7electron microscopy8.60W1-760[»]
5IY8electron microscopy7.90W1-760[»]
5IY9electron microscopy6.30W1-760[»]
ProteinModelPortaliP18074.
SMRiP18074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 283Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST277

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni438 – 637Mediates interaction with MMS19Add BLAST200

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi234 – 237DEAH box4
Motifi682 – 695Nuclear localization signalSequence analysisAdd BLAST14

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1131. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00550000075092.
HOGENOMiHOG000205390.
HOVERGENiHBG051498.
InParanoidiP18074.
KOiK10844.
OMAiAQDAMEM.
OrthoDBiEOG091G0262.
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. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. RAD3/XPD.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 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. AlignAdd to basket

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

        10         20         30         40         50
MKLNVDGLLV YFPYDYIYPE QFSYMRELKR TLDAKGHGVL EMPSGTGKTV
60 70 80 90 100
SLLALIMAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LNFYEKQEGE
110 120 130 140 150
KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQHDT
160 170 180 190 200
SLPHCRFYEE FDAHGREVPL PAGIYNLDDL KALGRRQGWC PYFLARYSIL
210 220 230 240 250
HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN
260 270 280 290 300
LTRRTLDRCQ GNLETLQKTV LRIKETDEQR LRDEYRRLVE GLREASAARE
310 320 330 340 350
TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV
360 370 380 390 400
QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEITD LADFSPLTLL
410 420 430 440 450
ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PILHFSCMDA SLAIKPVFER
460 470 480 490 500
FQSVIITSGT LSPLDIYPKI LDFHPVTMAT FTMTLARVCL CPMIIGRGND
510 520 530 540 550
QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT SYQYMESTVA
560 570 580 590 600
SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA
610 620 630 640 650
RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND
660 670 680 690 700
FLTFDAMRHA AQCVGRAIRG KTDYGLMVFA DKRFARGDKR GKLPRWIQEH
710 720 730 740 750
LTDANLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLESEETL
760
KRIEQIAQQL
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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00818747G → R in XP-D. 1
Natural variantiVAR_01728276T → A in XP-D. 1
Natural variantiVAR_003622112R → H in TTD1 and XP-D. 3 PublicationsCorresponds to variant rs121913020dbSNPEnsembl.1
Natural variantiVAR_011412199I → M.Corresponds to variant rs1799791dbSNPEnsembl.1
Natural variantiVAR_011413201H → Y.Corresponds to variant rs1799792dbSNPEnsembl.1
Natural variantiVAR_008188234D → N in XP-D. 1
Natural variantiVAR_008189259C → Y in TTD1. 1 PublicationCorresponds to variant rs370454709dbSNPEnsembl.1
Natural variantiVAR_011414312D → N.4 PublicationsCorresponds to variant rs1799793dbSNPEnsembl.1
Natural variantiVAR_003623461L → V in XP-D and TTD1. 3 PublicationsCorresponds to variant rs121913016dbSNPEnsembl.1
Natural variantiVAR_008190482Missing in TTD1. 1 Publication1
Natural variantiVAR_017283485L → P in XP-D; the corresponding mutation in fission yeast causes complete loss of activity. 1 PublicationCorresponds to variant rs121913025dbSNPEnsembl.1
Natural variantiVAR_017284487R → G in TTD1. 1
Natural variantiVAR_003624488 – 493Missing in TTD1; mild. 1 Publication6
Natural variantiVAR_017285511R → Q in XP-D. Corresponds to variant rs772572683dbSNPEnsembl.1
Natural variantiVAR_003625541S → R in XP-D; mild. 1 PublicationCorresponds to variant rs121913019dbSNPEnsembl.1
Natural variantiVAR_008191542Y → C in XP-D. 1
Natural variantiVAR_017286582 – 583EK → VSE in XP-D. 1 Publication2
Natural variantiVAR_017287592R → P in TTD1. 1
Natural variantiVAR_017288594A → P in TTD1. 1
Natural variantiVAR_008192601R → L in XP-D. Corresponds to variant rs140522180dbSNPEnsembl.1
Natural variantiVAR_017289601R → W in XP-D. Corresponds to variant rs753641926dbSNPEnsembl.1
Natural variantiVAR_003627602G → D in XP-D; combined with features of Cockayne syndrome. Corresponds to variant rs771824813dbSNPEnsembl.1
Natural variantiVAR_011415616R → C.1 Publication1
Natural variantiVAR_003626616R → P in XP-D and TTD1. 1 PublicationCorresponds to variant rs376556895dbSNPEnsembl.1
Natural variantiVAR_008193616R → W in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913024dbSNPEnsembl.1
Natural variantiVAR_008194658R → C in TTD1. 2 PublicationsCorresponds to variant rs121913021dbSNPEnsembl.1
Natural variantiVAR_017290658R → G in TTD1. 1
Natural variantiVAR_008195658R → H in TTD1. Corresponds to variant rs762141272dbSNPEnsembl.1
Natural variantiVAR_017291663C → R in TTD1. Corresponds to variant rs770367713dbSNPEnsembl.1
Natural variantiVAR_017292666R → W in XP-D. Corresponds to variant rs752510317dbSNPEnsembl.1
Natural variantiVAR_008196673D → G in TTD1. 1 Publication1
Natural variantiVAR_003628675G → R in XP-D/CS; severe form. 1 Publication1
Natural variantiVAR_017293681D → N in XP-D and COFS2. 1 PublicationCorresponds to variant rs121913023dbSNPEnsembl.1
Natural variantiVAR_008197683R → Q in XP-D. 1
Natural variantiVAR_008198683R → W in XP-D; 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. 1 PublicationCorresponds to variant rs41556519dbSNPEnsembl.1
Natural variantiVAR_008199713G → R in TTD1. 2 PublicationsCorresponds to variant rs121913022dbSNPEnsembl.1
Natural variantiVAR_003629716 – 730Missing in XP-D and TTD1. 1 PublicationAdd BLAST15
Natural variantiVAR_003630722R → W in TTD1. 2 PublicationsCorresponds to variant rs121913026dbSNPEnsembl.1
Natural variantiVAR_003631725A → P in TTD1. 1 PublicationCorresponds to variant rs121913018dbSNPEnsembl.1
Natural variantiVAR_011416751K → Q Polymorphism; may be associated with increased susceptibility to DNA damage. 6 PublicationsCorresponds to variant rs13181dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0431321 – 24Missing in isoform 2. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_043133414 – 429FTIII…TPTIA → QAQHCGSSRNQKRSHP in isoform 2. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_043134430 – 760Missing in isoform 2. 1 PublicationAdd BLAST331

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.487294.

Genome annotation databases

EnsembliENST00000391945; ENSP00000375809; ENSG00000104884. [P18074-1]
ENST00000485403; ENSP00000431229; ENSG00000104884. [P18074-2]
GeneIDi2068.
KEGGihsa:2068.
UCSCiuc002pbj.3. human. [P18074-1]

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:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.487294.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IVWelectron microscopy10.00W1-760[»]
5IY6electron microscopy7.20W1-760[»]
5IY7electron microscopy8.60W1-760[»]
5IY8electron microscopy7.90W1-760[»]
5IY9electron microscopy6.30W1-760[»]
ProteinModelPortaliP18074.
SMRiP18074.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108380. 34 interactors.
DIPiDIP-644N.
IntActiP18074. 14 interactors.
MINTiMINT-3008891.
STRINGi9606.ENSP00000375809.

PTM databases

iPTMnetiP18074.
PhosphoSitePlusiP18074.

Polymorphism and mutation databases

BioMutaiERCC2.
DMDMi119540.

Proteomic databases

EPDiP18074.
MaxQBiP18074.
PaxDbiP18074.
PeptideAtlasiP18074.
PRIDEiP18074.

Protocols and materials databases

DNASUi2068.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000391945; ENSP00000375809; ENSG00000104884. [P18074-1]
ENST00000485403; ENSP00000431229; ENSG00000104884. [P18074-2]
GeneIDi2068.
KEGGihsa:2068.
UCSCiuc002pbj.3. human. [P18074-1]

Organism-specific databases

CTDi2068.
DisGeNETi2068.
GeneCardsiERCC2.
GeneReviewsiERCC2.
HGNCiHGNC:3434. ERCC2.
HPAiCAB005375.
HPA038057.
MalaCardsiERCC2.
MIMi126340. gene.
278730. phenotype.
601675. phenotype.
610756. phenotype.
neXtProtiNX_P18074.
OpenTargetsiENSG00000104884.
Orphaneti1466. COFS syndrome.
33364. Trichothiodystrophy.
276258. Xeroderma pigmentosum complementation group D.
PharmGKBiPA27848.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1131. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00550000075092.
HOGENOMiHOG000205390.
HOVERGENiHBG051498.
InParanoidiP18074.
KOiK10844.
OMAiAQDAMEM.
OrthoDBiEOG091G0262.
PhylomeDBiP18074.
TreeFamiTF101232.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104884-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-2564830. Cytosolic iron-sulfur cluster assembly.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SIGNORiP18074.

Miscellaneous databases

ChiTaRSiERCC2. human.
GeneWikiiERCC2.
GenomeRNAii2068.
PROiP18074.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104884.
CleanExiHS_ERCC2.
ExpressionAtlasiP18074. baseline and differential.
GenevisibleiP18074. HS.

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. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. RAD3/XPD.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 203 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, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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