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Q9QXK2

- RAD18_MOUSE

UniProt

Q9QXK2 - RAD18_MOUSE

Protein

E3 ubiquitin-protein ligase RAD18

Gene

Rad18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri25 – 6440RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri201 – 22424UBZ-typeAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. ligase activity Source: UniProtKB-KW
    3. polyubiquitin binding Source: UniProtKB
    4. protein binding Source: MGI
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. DNA repair Source: UniProtKB-KW
    3. negative regulation of DNA recombination Source: MGI
    4. protein ubiquitination Source: UniProtKB-UniPathway
    5. response to UV Source: MGI
    6. spermatogenesis Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RAD18 (EC:6.3.2.-)
    Alternative name(s):
    Postreplication repair protein RAD18
    Short name:
    mRAD18Sc
    Gene namesi
    Name:Rad18
    Synonyms:Rad18sc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1890476. Rad18.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: MGI
    2. nucleus Source: MGI
    3. XY body Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509E3 ubiquitin-protein ligase RAD18PRO_0000056150Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei99 – 991PhosphoserineBy similarity
    Modified residuei103 – 1031PhosphoserineBy similarity
    Modified residuei164 – 1641PhosphoserineBy similarity
    Modified residuei485 – 4851PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9QXK2.
    PRIDEiQ9QXK2.

    PTM databases

    PhosphoSiteiQ9QXK2.

    Expressioni

    Tissue specificityi

    Expressed in thymus, spleen, brain, and ovary.

    Gene expression databases

    ArrayExpressiQ9QXK2.
    BgeeiQ9QXK2.
    CleanExiMM_RAD18.
    GenevestigatoriQ9QXK2.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with UBE2A and UBE2B, one homodimer binding one molecule of UBE2B. Interacts with HLTF and SHPRH. Interacts with SPRTN; leading to enhance chromatin association of RAD18 and RAD18-mediated PCNA ubiquitination and translesion DNA synthesis By similarity.By similarity

    Protein-protein interaction databases

    BioGridi208379. 2 interactions.
    STRINGi10090.ENSMUSP00000070619.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QXK2.
    SMRiQ9QXK2. Positions 8-95.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini248 – 28235SAPPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi232 – 2409LR motif

    Sequence similaritiesi

    Belongs to the RAD18 family.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation
    Contains 1 UBZ-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri25 – 6440RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri201 – 22424UBZ-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5432.
    GeneTreeiENSGT00390000011230.
    HOGENOMiHOG000234845.
    HOVERGENiHBG054721.
    KOiK10627.
    PhylomeDBiQ9QXK2.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR003034. SAP_dom.
    IPR018957. Znf_C3HC4_RING-type.
    IPR006642. Znf_Rad18_put.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF02037. SAP. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00513. SAP. 1 hit.
    SM00734. ZnF_Rad18. 1 hit.
    [Graphical view]
    PROSITEiPS50800. SAP. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QXK2-1 [UniParc]FASTAAdd to Basket

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    MEVLAEPRWP PGLAVMKTID DLLRCGICFE YFNIAVIIPQ CSHNYCSLCI    50
    RKFLSYKTQC PTCCVAVTEP DLRNNRLLDE LVKSMNFART HLLQFALESP 100
    PISPVSSTSK KVVVKVHNAD AAQHPVKQAN RLMDKFLIRE TGDCVFELLG 150
    KENERKFSPQ KELSTSAEIK ETSLLGKPVL GLSDANGPVT PSTSTMKLDT 200
    KVSCPVCGVS IPENHINKHL DSCLSREEKK ESLRSSAHKR KPLPKTVYNL 250
    LSDRDLKKKL KQYGLSVQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI 300
    VQEIESMEKT RMRLEASKLN ENVMVFTKNQ TEKEIEEVHS EYRKKHQNAF 350
    QLLVDQAKKG YKKTGRVSQA AAMRTDEPAE TLPSMRTDEP AETLPSMRTD 400
    EPAETLPLMR ADEPAETLPS ECIAQEDNVS FSDTVSVTNH FPQPQLDSPG 450
    PSEPERPDDS SSCTDILFSS DSDSCNRNDQ NREVSPQQTR RTRASECVEI 500
    EPRNKRNKN 509
    Length:509
    Mass (Da):57,412
    Last modified:June 6, 2002 - v2
    Checksum:iBF7717D1A69738F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91W → C in AAF19193. (PubMed:11013078)Curated
    Sequence conflicti268 – 2681Q → P in AAF19193. (PubMed:11013078)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF205278 mRNA. Translation: AAF19193.1.
    AK012795 mRNA. Translation: BAB28475.1.
    CCDSiCCDS39589.1.
    RefSeqiNP_067360.2. NM_021385.2.
    UniGeneiMm.103812.

    Genome annotation databases

    EnsembliENSMUST00000077088; ENSMUSP00000076341; ENSMUSG00000030254.
    GeneIDi58186.
    KEGGimmu:58186.
    UCSCiuc009dec.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF205278 mRNA. Translation: AAF19193.1 .
    AK012795 mRNA. Translation: BAB28475.1 .
    CCDSi CCDS39589.1.
    RefSeqi NP_067360.2. NM_021385.2.
    UniGenei Mm.103812.

    3D structure databases

    ProteinModelPortali Q9QXK2.
    SMRi Q9QXK2. Positions 8-95.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208379. 2 interactions.
    STRINGi 10090.ENSMUSP00000070619.

    PTM databases

    PhosphoSitei Q9QXK2.

    Proteomic databases

    MaxQBi Q9QXK2.
    PRIDEi Q9QXK2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077088 ; ENSMUSP00000076341 ; ENSMUSG00000030254 .
    GeneIDi 58186.
    KEGGi mmu:58186.
    UCSCi uc009dec.2. mouse.

    Organism-specific databases

    CTDi 56852.
    MGIi MGI:1890476. Rad18.

    Phylogenomic databases

    eggNOGi COG5432.
    GeneTreei ENSGT00390000011230.
    HOGENOMi HOG000234845.
    HOVERGENi HBG054721.
    KOi K10627.
    PhylomeDBi Q9QXK2.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 314151.
    PROi Q9QXK2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QXK2.
    Bgeei Q9QXK2.
    CleanExi MM_RAD18.
    Genevestigatori Q9QXK2.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR003034. SAP_dom.
    IPR018957. Znf_C3HC4_RING-type.
    IPR006642. Znf_Rad18_put.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF02037. SAP. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00513. SAP. 1 hit.
    SM00734. ZnF_Rad18. 1 hit.
    [Graphical view ]
    PROSITEi PS50800. SAP. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of mRAD18Sc, a mouse homolog of the yeast postreplication repair gene RAD18."
      van der Laan R., Roest H.P., Hoogerbrugge J.W., Smit E.M.E., Slater R., Baarends W.M., Hoeijmakers J.H.J., Grootegoed J.A.
      Genomics 69:86-94(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    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: Embryo.

    Entry informationi

    Entry nameiRAD18_MOUSE
    AccessioniPrimary (citable) accession number: Q9QXK2
    Secondary accession number(s): Q9CZB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 103 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3