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ERC6L_DANRE
ID   ERC6L_DANRE             Reviewed;        1451 AA.
AC   A2BGR3; A7E225;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA excision repair protein ERCC-6-like;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q2NKX8};
DE   AltName: Full=ATP-dependent helicase ERCC6-like;
GN   Name=ercc6l; ORFNames=si:ch211-278b8.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-579.
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: DNA helicase that acts as a tension sensor that associates
CC       with catenated DNA which is stretched under tension until it is
CC       resolved during anaphase. Functions as ATP-dependent DNA translocase.
CC       Can promote Holliday junction branch migration (in vitro).
CC       {ECO:0000250|UniProtKB:Q2NKX8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q2NKX8};
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Note=Localizes to kinetochores, inner
CC       centromeres and thin threads connecting separating chromosomes even
CC       during anaphase. {ECO:0000250|UniProtKB:Q2NKX8}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; CR391924; CAM13192.1; -; Genomic_DNA.
DR   EMBL; BX510925; CAM13192.1; JOINED; Genomic_DNA.
DR   EMBL; BX510925; CAM14199.1; -; Genomic_DNA.
DR   EMBL; CR391924; CAM14199.1; JOINED; Genomic_DNA.
DR   EMBL; BC150168; AAI50169.1; -; mRNA.
DR   RefSeq; NP_001093563.1; NM_001100093.2.
DR   RefSeq; XP_009299551.1; XM_009301276.2.
DR   AlphaFoldDB; A2BGR3; -.
DR   SMR; A2BGR3; -.
DR   STRING; 7955.ENSDARP00000012447; -.
DR   iPTMnet; A2BGR3; -.
DR   PaxDb; A2BGR3; -.
DR   PeptideAtlas; A2BGR3; -.
DR   PRIDE; A2BGR3; -.
DR   Ensembl; ENSDART00000015401; ENSDARP00000012447; ENSDARG00000002479.
DR   GeneID; 100005291; -.
DR   KEGG; dre:100005291; -.
DR   CTD; 54821; -.
DR   ZFIN; ZDB-GENE-060531-56; ercc6l.
DR   eggNOG; KOG0387; Eukaryota.
DR   GeneTree; ENSGT00940000156837; -.
DR   HOGENOM; CLU_004666_0_0_1; -.
DR   InParanoid; A2BGR3; -.
DR   OMA; HDGESEM; -.
DR   OrthoDB; 372069at2759; -.
DR   PhylomeDB; A2BGR3; -.
DR   TreeFam; TF332843; -.
DR   Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:A2BGR3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000002479; Expressed in blastula and 28 other tissues.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW   DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..1451
FT                   /note="DNA excision repair protein ERCC-6-like"
FT                   /id="PRO_0000328833"
FT   REPEAT          27..60
FT                   /note="TPR 1"
FT   DOMAIN          118..286
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          479..639
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REPEAT          1402..1435
FT                   /note="TPR 2"
FT   REGION          647..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1063..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           237..240
FT                   /note="DEAH box"
FT   COMPBIAS        648..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..804
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1241..1301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1343
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         961
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   CONFLICT        45
FT                   /note="R -> H (in Ref. 2; AAI50169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="T -> A (in Ref. 2; AAI50169)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1451 AA;  163227 MW;  4BE27ACF410D1EDB CRC64;
     MESNNVEEVT DKFGGCLSLD TEKMGKYDRY RQKGKEAALN GELPRALELF QLAYQLQPSE
     KLKKRIQAIQ DLIQREDEED EEEEEEFVNV NNSGLKLYKG LYDKLYDHQK EGVAFLYSLY
     RDGRKGGILA DDMGLGKTIQ VISFLSGMYD AELANHTLLV MPTSLIKNWV REFAKWTPGM
     RVKEFHGSSK TERNRNLERI QRKGGVIITT YQMLINNYEQ LGSNGHREFK WDYVILDEAH
     KIKTSSTKTA KSAHAIPAKN RVLLTGTPVQ NNLREMWALF DFACQGSLLG TSKTFKTEYE
     NPITRAREKD ATPGEKALGL RISQNLTDII KPYFLRRTKA DVQQKKLKLE EGFEEEEDQE
     NKCPNAREGV EMPSLTRKND LIVWTYLSSV QEDIYNKFIS LDQIKELLTT TRSPLAELTV
     LKKLCDHPRL LSQRAVIQLG LERGSDSELV HSDESESAVS QIDNISDHTL IEESGKLQFV
     VSLMECLREE GHRTLIFSQS RKMLDIMERV LRNRNFRLLR LDGTVTQLAE REKRISLFQT
     DKRYTIFLLT TQVGGVGITL TGANRVVIFD PSWNPATDAQ AVDRAYRIGQ TENVIIYRLI
     TCGTVEEKIY RRQVFKDSLI RQTTGDKKNP FRYFSKQELR ELFKLEDTRS SSTQQQLQAM
     HAQSRRSDTS LDHHIARLHS MEMFGISDHD LMFTKEPAAD EDDPEDAESH HYIQTRVQKA
     QELMQAESEL HGQLLDSMAQ NTEPAWLRQM GQPNSSIRDR PAPPRIKNEP VTVDLTHNSF
     DEPEFEEDEQ NLPSAEDAEM ETASEDVEVI GDEDLGDKVI SSEVEVVGEE VEVVAEEVED
     AGEVEVVSEE VEGVGVEVED VGVEVEDAGV EVEDAGVEVE DAGVEVEDAG EVEVVSGEGQ
     VQPKSPQSGG EWNLQIVKTE VSPIAEKFAD VITLDDTSDE ADSSDFNTES KQQNSSQRFQ
     SPSLQFPKLD DLSGASNTLG NEEVEPEKCH SQVLSSPLSQ HEATTDEPFK AEMEMPHGNF
     NLLLEDSADM YFPEDEEVHE VEESAAEESP EFQLQMDVSG ERLEEPSINH DKQNNGEFVN
     YNDSEVSKRE SLLKIRSTPN ESVDDSFVHS VRTKKRQVIS DTEEEEEEEE ESEKPCLTSS
     PFIDAISRLG SSTPKAVLVD GARLRRSLNA SVASRRSFVV SLLENESDEE SNEDKTKSSG
     ASETCADELV EEVQTSSGDN SKSYETSEAN GTLADELVEE EGEYREGKNT SDKVSESNET
     HSEEFAEEEK PSGDKSESYE ISEASETHTD NSEEEIIGDH TGSYKISESS EADESVVEEE
     EPSGETLNTE ESEMGEEEES AELIAGQEQE EWHSAVLEST GDVELDSNET MDQCAPKTVP
     VETHVLPVSS TNTAAEASDN KYNLLVLSGK QSLAEGRKQE ALDFFLKAID INTGDPEIQL
     LIIQLYRQLS Q
 
 
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