NSE1_DROME
ID NSE1_DROME Reviewed; 235 AA.
AC Q9VMA0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Non-structural maintenance of chromosomes element 1 homolog;
DE Short=Non-SMC element 1 homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN Name=Nse1 {ECO:0000312|FlyBase:FBgn0031848};
GN ORFNames=CG11329 {ECO:0000312|FlyBase:FBgn0031848};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP FUNCTION, IDENTIFICATION IN SMC5-SMC6 COMPLEX, AND INTERACTION WITH MAGE.
RX PubMed=23555814; DOI=10.1371/journal.pone.0059866;
RA Li X., Zhuo R., Tiong S., Di Cara F., King-Jones K., Hughes S.C.,
RA Campbell S.D., Wevrick R.;
RT "The Smc5/Smc6/MAGE complex confers resistance to caffeine and genotoxic
RT stress in Drosophila melanogaster.";
RL PLoS ONE 8:E59866-E59866(2013).
CC -!- FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in
CC repair of DNA double-strand breaks by homologous recombination
CC (PubMed:23555814). The complex may promote sister chromatid homologous
CC recombination by recruiting the SMC1-SMC3 cohesin complex to double-
CC strand breaks (By similarity). {ECO:0000250|UniProtKB:Q8WV22,
CC ECO:0000269|PubMed:23555814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WV22};
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists at least of
CC Smc5, Smc6, Nse1, Nse2, Nse4 and MAGE. Nse1, Nse4 and MAGE probably
CC form a subcomplex that bridges the head domains of the Smc5-Smc6
CC heterodimer (By similarity). Interacts with MAGE and Nse4.
CC {ECO:0000250|UniProtKB:Q8WV22, ECO:0000269|PubMed:23555814}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF52422.1; -; Genomic_DNA.
DR EMBL; AY051646; AAK93070.1; -; mRNA.
DR RefSeq; NP_001260145.1; NM_001273216.1.
DR RefSeq; NP_609063.1; NM_135219.3.
DR AlphaFoldDB; Q9VMA0; -.
DR SMR; Q9VMA0; -.
DR BioGRID; 60091; 2.
DR IntAct; Q9VMA0; 1.
DR STRING; 7227.FBpp0305541; -.
DR iPTMnet; Q9VMA0; -.
DR PaxDb; Q9VMA0; -.
DR DNASU; 33938; -.
DR EnsemblMetazoa; FBtr0079319; FBpp0078948; FBgn0031848.
DR EnsemblMetazoa; FBtr0333349; FBpp0305541; FBgn0031848.
DR GeneID; 33938; -.
DR KEGG; dme:Dmel_CG11329; -.
DR UCSC; CG11329-RA; d. melanogaster.
DR CTD; 33938; -.
DR FlyBase; FBgn0031848; Nse1.
DR VEuPathDB; VectorBase:FBgn0031848; -.
DR eggNOG; KOG4718; Eukaryota.
DR GeneTree; ENSGT00390000009084; -.
DR HOGENOM; CLU_045153_3_0_1; -.
DR InParanoid; Q9VMA0; -.
DR OMA; QMGYFME; -.
DR OrthoDB; 1159451at2759; -.
DR PhylomeDB; Q9VMA0; -.
DR BioGRID-ORCS; 33938; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33938; -.
DR PRO; PR:Q9VMA0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031848; Expressed in ovary and 9 other tissues.
DR ExpressionAtlas; Q9VMA0; baseline and differential.
DR Genevisible; Q9VMA0; DM.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006281; P:DNA repair; ISS:FlyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:FlyBase.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR014857; Znf_RING-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR20973; PTHR20973; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
DR Pfam; PF08746; zf-RING-like; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..235
FT /note="Non-structural maintenance of chromosomes element 1
FT homolog"
FT /id="PRO_0000372845"
FT ZN_FING 181..225
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 235 AA; 26774 MW; B390DF621FC0C002 CRC64;
MELVKRGFLR ACKNHSYLSF ELIDDILAPL CANHKTTKPG SKEAIRALVA EINDTISDLG
QLLVFIKYPV KAEEYLVYAK TDATPDSVAN TGLTAEECQY FSKLLDKIAS EEDCHIAWND
AYNDIVLQAS SKPLKKSRMQ ELLQKWIQMG YFMEVTDRIY LGPRSLVELS FYLSSNHADN
IKNCTLCKCL VLWDIRCGSC NIQYHRGCIQ TYLQRRDICP SCGNLWTTPI RRSIG
