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O08811

- ERCC2_MOUSE

UniProt

O08811 - ERCC2_MOUSE

Protein

TFIIH basal transcription factor complex helicase XPD subunit

Gene

Ercc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Magnesium.By similarity
    Binds 1 4Fe-4S cluster.By similarity

    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)By similarity

    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. metal ion binding Source: UniProtKB-KW
    7. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl

    GO - Biological processi

    1. aging Source: MGI
    2. apoptotic process Source: UniProtKB
    3. ATP catabolic process Source: GOC
    4. bone mineralization Source: MGI
    5. cell proliferation Source: MGI
    6. central nervous system myelin formation Source: MGI
    7. chromosome segregation Source: UniProtKB
    8. DNA duplex unwinding Source: GOC
    9. DNA repair Source: MGI
    10. embryonic cleavage Source: MGI
    11. erythrocyte maturation Source: MGI
    12. extracellular matrix organization Source: MGI
    13. hair cell differentiation Source: MGI
    14. hair cycle process Source: MGI
    15. hair follicle maturation Source: MGI
    16. hematopoietic stem cell differentiation Source: MGI
    17. in utero embryonic development Source: MGI
    18. multicellular organism growth Source: MGI
    19. nucleotide-excision repair Source: MGI
    20. nucleotide-excision repair, DNA incision Source: Ensembl
    21. positive regulation of DNA binding Source: MGI
    22. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    23. post-embryonic development Source: MGI
    24. regulation of mitotic cell cycle phase transition Source: Ensembl
    25. response to hypoxia Source: Ensembl
    26. response to oxidative stress Source: MGI
    27. response to UV Source: MGI
    28. skin development Source: MGI
    29. spinal cord development Source: MGI
    30. transcription-coupled nucleotide-excision repair Source: UniProtKB
    31. transcription from RNA polymerase II promoter Source: UniProtKB
    32. UV protection Source: MGI

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Chromosome partition, DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_196637. Cytosolic iron-sulfur cluster assembly.
    REACT_203462. Formation of the Early Elongation Complex.
    REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_224562. Dual incision reaction in TC-NER.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TFIIH basal transcription factor complex helicase XPD subunit (EC:3.6.4.12)
    Alternative name(s):
    CXPD
    DNA excision repair protein ERCC-2
    DNA repair protein complementing XP-D cells
    Xeroderma pigmentosum group D-complementing protein
    Gene namesi
    Name:Ercc2
    Synonyms:Xpd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95413. Ercc2.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonspindle By similarity

    GO - Cellular componenti

    1. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. holo TFIIH complex Source: UniProtKB
    4. MMXD complex Source: UniProtKB
    5. nucleus Source: MGI
    6. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760TFIIH basal transcription factor complex helicase XPD subunitPRO_0000101981Add
    BLAST

    Post-translational modificationi

    ISGylated.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiO08811.
    PRIDEiO08811.

    PTM databases

    PhosphoSiteiO08811.

    Expressioni

    Gene expression databases

    BgeeiO08811.
    GenevestigatoriO08811.

    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 By similarity. Interacts with ATF7IP By similarity.By similarity

    Protein-protein interaction databases

    IntActiO08811. 1 interaction.
    MINTiMINT-4114299.
    STRINGi10090.ENSMUSP00000054380.

    Structurei

    3D structure databases

    ProteinModelPortaliO08811.
    SMRiO08811. Positions 26-258.
    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 MMS19By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi234 – 2374DEAH box

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1199.
    GeneTreeiENSGT00550000075092.
    HOGENOMiHOG000205390.
    HOVERGENiHBG051498.
    InParanoidiQ8C487.
    KOiK10844.
    OMAiDEVWKYK.
    OrthoDBiEOG70W3CM.
    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]

    Sequencei

    Sequence statusi: Complete.

    O08811-1 [UniParc]FASTAAdd to Basket

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    MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV    50
    SLLALIVAYQ RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE 100
    KLPFLGLALS SRKNLCIHPE VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA 150
    SLPHCRFYEE FDIHGRQMPL PAGIYNLDDL KALGQRQGWC PYFLARYSIL 200
    HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID NVCIDSMSVN 250
    LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASVARE 300
    TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV 350
    QESPPAFLSG LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL 400
    ANFATLVSTY AKGFTIIIEP FDDRTPTIAN PVLHFSCMDA 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 DKRFARADKR GKLPRWIQEH 700
    LTDSNLNLTV DEGVQVAKYF LRQMAQPFHR EDQLGLSLLS LEQLQSEETL 750
    QRIEQIAQQL 760
    Length:760
    Mass (Da):86,842
    Last modified:July 27, 2011 - v2
    Checksum:i02B2E116792D4E44
    GO

    Sequence cautioni

    The sequence BAB23443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti285 – 2851Y → C in BAB23443. (PubMed:16141072)Curated
    Sequence conflicti595 – 5951I → V in AAB58296. (PubMed:9426063)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97572 mRNA. Translation: AAB58296.1.
    AK004652 mRNA. Translation: BAB23443.1. Different initiation.
    AK082761 mRNA. Translation: BAC38607.1.
    CH466639 Genomic DNA. Translation: EDL23140.1.
    CCDSiCCDS20900.1.
    RefSeqiNP_031975.2. NM_007949.4.
    UniGeneiMm.36524.

    Genome annotation databases

    EnsembliENSMUST00000062831; ENSMUSP00000054380; ENSMUSG00000030400.
    GeneIDi13871.
    KEGGimmu:13871.
    UCSCiuc009flq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97572 mRNA. Translation: AAB58296.1 .
    AK004652 mRNA. Translation: BAB23443.1 . Different initiation.
    AK082761 mRNA. Translation: BAC38607.1 .
    CH466639 Genomic DNA. Translation: EDL23140.1 .
    CCDSi CCDS20900.1.
    RefSeqi NP_031975.2. NM_007949.4.
    UniGenei Mm.36524.

    3D structure databases

    ProteinModelPortali O08811.
    SMRi O08811. Positions 26-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O08811. 1 interaction.
    MINTi MINT-4114299.
    STRINGi 10090.ENSMUSP00000054380.

    PTM databases

    PhosphoSitei O08811.

    Proteomic databases

    PaxDbi O08811.
    PRIDEi O08811.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000062831 ; ENSMUSP00000054380 ; ENSMUSG00000030400 .
    GeneIDi 13871.
    KEGGi mmu:13871.
    UCSCi uc009flq.1. mouse.

    Organism-specific databases

    CTDi 2068.
    MGIi MGI:95413. Ercc2.

    Phylogenomic databases

    eggNOGi COG1199.
    GeneTreei ENSGT00550000075092.
    HOGENOMi HOG000205390.
    HOVERGENi HBG051498.
    InParanoidi Q8C487.
    KOi K10844.
    OMAi DEVWKYK.
    OrthoDBi EOG70W3CM.
    TreeFami TF101232.

    Enzyme and pathway databases

    Reactomei REACT_196637. Cytosolic iron-sulfur cluster assembly.
    REACT_203462. Formation of the Early Elongation Complex.
    REACT_223654. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_224562. Dual incision reaction in TC-NER.
    REACT_226490. RNA Polymerase II Transcription Elongation.

    Miscellaneous databases

    NextBioi 284788.
    PROi O08811.
    SOURCEi Search...

    Gene expression databases

    Bgeei O08811.
    Genevestigatori O08811.

    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. "Disruption of the mouse xeroderma pigmentosum group D DNA repair/basal transcription gene results in preimplantation lethality."
      de Boer J., Donker I., de Wit J., Hoeijmakers J.H.J., Weeda G.
      Cancer Res. 58:89-94(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Lung.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiERCC2_MOUSE
    AccessioniPrimary (citable) accession number: O08811
    Secondary accession number(s): Q8C487, Q9DC01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3