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Q8BHK9

- ERC6L_MOUSE

UniProt

Q8BHK9 - ERC6L_MOUSE

Protein

DNA excision repair protein ERCC-6-like

Gene

Ercc6l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi123 – 1308ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: UniProtKB-KW

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA excision repair protein ERCC-6-like (EC:3.6.4.12)
    Alternative name(s):
    ATP-dependent helicase ERCC6-like
    Gene namesi
    Name:Ercc6l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:2654144. Ercc6l.

    Subcellular locationi

    Chromosomecentromere By similarity. Chromosomecentromerekinetochore By similarity
    Note: Localizes to kinetochores, inner centromeres and thin threads connecting separating chromosomes even during anaphase. In prometaphase cells, it mostly concentrates in between kinetochores. In metaphase, it localizes to numerous thin threads that stretch between sister kinetochores of the aligned chromosomes and are composed of catenated centromeric DNA. Evolution from inner centromeres to thin threads takes place in response to tension. Resolution of thin threads requires topoisomerase 2-alpha (TOP2A) after anaphase onset By similarity.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12401240DNA excision repair protein ERCC-6-likePRO_0000328832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141PhosphoserineBy similarity
    Modified residuei755 – 7551PhosphoserineBy similarity
    Modified residuei773 – 7731PhosphoserineBy similarity
    Modified residuei821 – 8211PhosphoserineBy similarity
    Modified residuei1021 – 10211Phosphoserine1 Publication
    Modified residuei1057 – 10571PhosphothreonineBy similarity
    Modified residuei1092 – 10921PhosphoserineBy similarity
    Modified residuei1172 – 11721PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by PLK1 prevents the association with chromosome arms and restricts its localization to the kinetochore-centromere region.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BHK9.
    PaxDbiQ8BHK9.
    PRIDEiQ8BHK9.

    PTM databases

    PhosphoSiteiQ8BHK9.

    Expressioni

    Tissue specificityi

    Expressed mainly in the neural tube and heart of E10.5 embryo. Significantly down-regulated after alcohol exposure in embryonic brain and heart, but not in embryonic kidney, liver, or lung.1 Publication

    Gene expression databases

    ArrayExpressiQ8BHK9.
    BgeeiQ8BHK9.
    GenevestigatoriQ8BHK9.

    Interactioni

    Subunit structurei

    Interacts with PLK1, which phosphorylates it. Both proteins are mutually dependent on each other for correct subcellular localization By similarity.By similarity

    Protein-protein interaction databases

    BioGridi231820. 7 interactions.
    IntActiQ8BHK9. 7 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BHK9.
    SMRiQ8BHK9. Positions 100-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati21 – 5434TPR 1Add
    BLAST
    Domaini110 – 278169Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini467 – 631165Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati1191 – 122434TPR 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi229 – 2324DEAH box

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 2 TPR repeats.Curated

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00590000083118.
    HOGENOMiHOG000074172.
    HOVERGENiHBG107854.
    InParanoidiQ8BHK9.
    OMAiICEMPSL.
    OrthoDBiEOG76DTRN.
    PhylomeDBiQ8BHK9.
    TreeFamiTF332843.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProiIPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BHK9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEASQGLAEV ETLSPQLAES YLRYVQEAKE AAKNGDLEES LKLFNLAKDI     50
    FPTKKVMSRI QKLQEALEQL AEEEDDDEFI DVCSSGLLLY RELYEKLFEH 100
    QKEGIAFLYS LYKDGRKGGI LADDMGLGKT VQIIAFLSGM FDASLVNHVL 150
    LIMPTNLINT WVNEFAKWTP GMRVKTFHGS SKSERTRSLT RIQQRNGVVI 200
    TTYQMLLNNW QQLASFNGQA FVWDYVILDE AHKIKSASTK SAVCARAIPA 250
    SNRLLLTGTP VQNNLQELWS LFDFACQGSL LGTLKTFKME YEHPIIRARE 300
    KDATPGEKAL GLKISENLME IIKPYFLRRT KEEVQTKKAD NPEARLGEKN 350
    PAGEAICDMF SLARKNDLIV WIRLLPLQEE IYRKFVSLDH IKELLMETRS 400
    PLAELGVLKK LCDHPRLLSA RACRLLNLGT ATFSAQDENE QEDVSNMNSI 450
    DHLPDKTLIQ ESGKMIFLMS LLERLQDEGH QTLVFSQSIK ILNIIERLLK 500
    NKHFKTLRID GTVTHLWERE KRIQLFQQNK EYSVFLLTTQ VGGVGLTLTA 550
    ATRVVIFDPS WNPATDAQAV DRVYRIGQKE NVVVYRLITC GTVEEKIYRR 600
    QVFKDSLIRQ TTGEKKNPFR YFTKQELKEL FTVGDLQKSA TQMQLQCLHA 650
    AQRRSDEKLD EHIAYLHLLG IAGISDHDLM FTRDLSVKEE LDMLEDSQYI 700
    HQRVQKAQFL VESESQNTVQ RQTTGIEETW LKAQEFPSQQ KKKGTEFNKP 750
    QPQPSRLLTK PTQVEAISSQ MASITICDQS AESEPQEHSE VHDVTSLQGS 800
    HHFNSTSDAG TIASLPQGAE SIGEVSTDSL LSPAKGFAAE NDAMQKKGLQ 850
    ASPGQEAPSE NLGSFHYLPR ESSKASLGPN LDLQDSVVLY HRSPTANENQ 900
    NLESDVPMIE ISDDLSEPPS ALQGAQAIEA QLELKEDDPL KSPPQYACDF 950
    NLFLEDSADT RQNLSSKFLE HVEKEKSLQS PAANSRAKSA LTLSLDSSPK 1000
    SDEESEVISV KTKSKTRRIL SDDEDEDEED AFKGSHTNSI NISPFPFSSV 1050
    KQFDASTPQS GSNPSRRFFS PKTPGEVNTS LHSRRSLASR RSLINVVLDD 1100
    VEDMEERLDN SSEEESEPGL SEENNEEEAL ACTEEQPSGA TLASGNKSSN 1150
    LTMSEPTSPA PQSSPCAPEP SSSDPMPDPP QDLAVEAGND YESLVARGKE 1200
    LKECGKIQEA LNCLVKALDI KSADPEVMLM TLSLYKQLNI 1240
    Length:1,240
    Mass (Da):138,854
    Last modified:March 1, 2003 - v1
    Checksum:i0B996A4286F51C27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1210 – 12101A → S in BAC26244. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY172688 mRNA. Translation: AAN87172.1.
    AK029015 mRNA. Translation: BAC26244.1.
    AK045113 mRNA. Translation: BAC32227.2.
    AK084617 mRNA. Translation: BAC39230.1.
    AK084618 mRNA. Translation: BAC39231.1.
    AL807784 Genomic DNA. Translation: CAM24634.1.
    BC037660 mRNA. Translation: AAH37660.1.
    CCDSiCCDS30321.1.
    RefSeqiNP_666347.2. NM_146235.3.
    UniGeneiMm.31911.

    Genome annotation databases

    EnsembliENSMUST00000056904; ENSMUSP00000050592; ENSMUSG00000051220.
    GeneIDi236930.
    KEGGimmu:236930.
    UCSCiuc009tyk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY172688 mRNA. Translation: AAN87172.1 .
    AK029015 mRNA. Translation: BAC26244.1 .
    AK045113 mRNA. Translation: BAC32227.2 .
    AK084617 mRNA. Translation: BAC39230.1 .
    AK084618 mRNA. Translation: BAC39231.1 .
    AL807784 Genomic DNA. Translation: CAM24634.1 .
    BC037660 mRNA. Translation: AAH37660.1 .
    CCDSi CCDS30321.1.
    RefSeqi NP_666347.2. NM_146235.3.
    UniGenei Mm.31911.

    3D structure databases

    ProteinModelPortali Q8BHK9.
    SMRi Q8BHK9. Positions 100-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 231820. 7 interactions.
    IntActi Q8BHK9. 7 interactions.

    PTM databases

    PhosphoSitei Q8BHK9.

    Proteomic databases

    MaxQBi Q8BHK9.
    PaxDbi Q8BHK9.
    PRIDEi Q8BHK9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056904 ; ENSMUSP00000050592 ; ENSMUSG00000051220 .
    GeneIDi 236930.
    KEGGi mmu:236930.
    UCSCi uc009tyk.2. mouse.

    Organism-specific databases

    CTDi 54821.
    MGIi MGI:2654144. Ercc6l.

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00590000083118.
    HOGENOMi HOG000074172.
    HOVERGENi HBG107854.
    InParanoidi Q8BHK9.
    OMAi ICEMPSL.
    OrthoDBi EOG76DTRN.
    PhylomeDBi Q8BHK9.
    TreeFami TF332843.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Miscellaneous databases

    NextBioi 383173.
    PROi Q8BHK9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BHK9.
    Bgeei Q8BHK9.
    Genevestigatori Q8BHK9.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression analysis of mouse gene encoding the protein Ercc6l which is a novel member of SNF2 family."
      Chen X.-G., Li Y., Zang M.-X., Pei X.-R., Xu Y.-J., Fang L.-F.
      Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:443-448(2004)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Heart.
    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, Heart and Skin.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "Ercc6l, a gene of SNF2 family, may play a role in the teratogenic action of alcohol."
      Xu Y.-J., Chen X.-G., Li Y.
      Toxicol. Lett. 157:233-239(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiERC6L_MOUSE
    AccessioniPrimary (citable) accession number: Q8BHK9
    Secondary accession number(s): Q8BGN1, Q8BRC9, Q8CE49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 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