GenomeNet

Database: UniProt
Entry: F7EMA8_MACMU
LinkDB: F7EMA8_MACMU
Original site: F7EMA8_MACMU 
ID   F7EMA8_MACMU            Unreviewed;      2061 AA.
AC   F7EMA8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=ERCC excision repair 6, chromatin remodeling factor {ECO:0000313|Ensembl:ENSMMUP00000023587.4};
GN   Name=ERCC6 {ECO:0000313|Ensembl:ENSMMUP00000023587.4,
GN   ECO:0000313|VGNC:VGNC:81396};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000023587.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000023587.4, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000023587.4,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000023587.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000023587.4};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   RefSeq; XP_015002505.1; XM_015147019.1.
DR   RefSeq; XP_015002506.1; XM_015147020.1.
DR   RefSeq; XP_015002507.1; XM_015147021.1.
DR   RefSeq; XP_015002508.1; XM_015147022.1.
DR   STRING; 9544.ENSMMUP00000023587; -.
DR   Ensembl; ENSMMUT00000025211.4; ENSMMUP00000023587.4; ENSMMUG00000017943.4.
DR   VEuPathDB; HostDB:ENSMMUG00000017943; -.
DR   VGNC; VGNC:81396; ERCC6.
DR   GeneTree; ENSGT00940000158057; -.
DR   HOGENOM; CLU_000315_7_3_1; -.
DR   InParanoid; F7EMA8; -.
DR   OMA; VKHDAIM; -.
DR   Proteomes; UP000006718; Chromosome 9.
DR   Bgee; ENSMMUG00000017943; Expressed in fibroblast and 22 other cell types or tissues.
DR   ExpressionAtlas; F7EMA8; baseline.
DR   GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR   GO; GO:0008023; C:transcription elongation factor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
DR   GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IEA:Ensembl.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0000303; P:response to superoxide; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   GO; GO:0006362; P:transcription elongation by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR   CDD; cd21397; cc_ERCC-6_N; 1.
DR   CDD; cd22254; CSB_WHD; 1.
DR   CDD; cd18000; DEXHc_ERCC6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029526; PGBD.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF13843; DDE_Tnp_1_7; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN          1087..1263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1411..1570
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1610..1815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1887..1949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..339
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..399
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1648..1709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1710..1724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1726..1742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1743..1770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1779..1815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1899..1921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1922..1943
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2061 AA;  233145 MW;  067FEDDA9FA6B022 CRC64;
     MPNEGIPHSS QTQEQDYLQS QPVSNNEEMA IKQESGGDGE VEEYLPFSSV GDGPSTSAEG
     CASAASRRGP ALLHINRHQI QAVEPSAQAL ELQGLGVDVY DQDVLEQGVL RQVDNAIHEA
     SRTSQLADVE KEYRSVLDDL TSCTTSLRQI NKIIEQLSPQ AATSRDINRK LDSVKRQKYN
     KEQQLKKITA KQKHLQAILG GAEVKIELDH ASLEEDAEPG PSSLGSMLMP VQETAWEELI
     RTGQMTPFGT QIPQKQEKKP RKIMLNEASG FEKYLADQAK LSFERKKQAT CNKRPARKAP
     ASVTPPAPTQ SKNKPNKKAK VLSKKEERLK KHIKKLQKRA LQFQGKVGLP KARRPWESDM
     RPEAEGDSEG EESEYFPTEE EEEEEEEDDE VEGVEADLSG DGTDYELKPL PKGRKRQKKV
     PVQEIDDDFF PSSGEEAEAS PIGEGGGGGR KVGRYRDDGD EDYYKQRLSP KMPRTLSLHE
     ITDLLETDDS IEASAIVIQP PENATAPVSD EESGDEEGGT INNLPGSLLH TAAYLIQDGS
     DAESDSDDPS YAPKDDSPDE VPSTSSVQQP PPSRRRKMTK IVCKWKKADL TVQPVAGRVT
     APPNDFFTEM RTPTEILELF LDDEVIELIV KYSNLYADSK GVHLGLTSSE FKCFLGIIFL
     SGYVSVPRRR MFWEQRTDVH NVLVSAAMRR DRFETIFSNL HVADNADLDP VDKFSKLRPL
     ISKLNERCMK FVPNETYFSF DEFMVPYFGR HGCKQFIRGK PIRFGYKFWC GATCLGYICW
     FQPYQGKNPN TKHEEYGVGA SLVLQFSEAL TEAHPGRYHF VFNNFFTSIA LLDKLSSMGH
     QATGTVRKDH IDKVPLESDV ALKKKERGTF DYRIDGKGNI VCRWNDNSVV TVASSGAGIH
     PLCLVSRYSQ KLKKKIQVQQ PNMIKVYNQF MGGVDRADEN IDKYRASIRG KKWYSSPLLF
     CFELVLQNAW QLHKTYDEKP VDFLEFRRRV VCHYLETHGH PPEPGQKGRP QKRNIDSRYD
     GINHVIVKQG KQTRRWNKLR LQDKEKRLKL EDDSEESDAE FDEGFKVPGF LFKKLFKYQQ
     TGVRWLWELH CQQAGGILGD EMGLGKTIQI IAFLAGLSYS KIRTRGSNYR FEGLGPTVIV
     CPTTVMHQWV KEFHTWWPPF RVAILHETGS YTHKKEKLIR DVAHCHGILI TSYSYIRLMQ
     DDISRYDWHY VILDEGHKIR NPNAAVTLAC KQFRTPHRII LSGSPMQNNL RELWSLFDFI
     FPGKLGTLPV FMEQFSVPIT MGGYSNASPV QVKTAYKCAC VLRDTINPYL LRRMKSDVKM
     SLSLPDKNEQ VLFCRLTDEQ HKVYQNFVDS KEVYRILNGE MQIFSGLIAL RKICNHPDLF
     SGGPKNLKGL PDDELEEDQF GYWKRSGKMI VVESLLKIWH KQGQRVLLFS QSRQMLDILE
     VFLRAQKYTY LKMDGTTTIA SRQPLITRYN EDTSIFVFLL TTRVGGLGVN LTGANRVVIY
     DPDWNPSTDT QARERAWRIG QKKQVTVYRL LTAGTIEEKI YHRQIFKQFL TNRVLKDPKQ
     RRFFKSNDLY ELFTLTSPDA SQSTETSAIF AGTGSDVQTP KCHLKRKIQP AFGADHDVPK
     RKKFPASNIS INDATSSEEK SEAKGAEVNV VPSNQSDPLK DDPHMSSNIA SNDRLGGETN
     AVSGLEESSV ISGNRECSNS SGTGKTSRPS GDESIDEKLG LSYKRERPSQ AQTESFWENK
     QMENNFYKHK SKTKHHSVAE EETLEKHLRP KQKPKNPKHC RDAKFEGTRI PHLVKKRRYQ
     KQDSENKSEA KEQSNDDYVL EKLFKKSVGV HSVMKHDAIM DGASPDYVLV EAEANRVAQD
     ALKALRLSRQ RCLGAVSGVP TWTGHRGISG APAGTKSRFG KKRNSNFSVQ HSSSTSPTEK
     CQDGIMKKEG KDNVPEHFSG RAEDADSSSG ALASSSLLAK MRARNHLILP ERLESESGHL
     QEASALLPTT EHDDLLVEMR NFIAFQAHTD GQASTREILQ EFESKLSASQ SCVFRELLRN
     LCTFHRTSGG EGIWKLKPEY C
//
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