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NSE1_YEAST
ID   NSE1_YEAST              Reviewed;         336 AA.
AC   Q07913; D6VY09;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Non-structural maintenance of chromosomes element 1;
DE            Short=Non-SMC element 1;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN   Name=NSE1; OrderedLocusNames=YLR007W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, INTERACTION WITH SMC5 AND SMC6, AND SUBCELLULAR LOCATION.
RX   PubMed=11927594; DOI=10.1074/jbc.m201523200;
RA   Fujioka Y., Kimata Y., Nomaguchi K., Watanabe K., Kohno K.;
RT   "Identification of a novel non-structural maintenance of chromosomes (SMC)
RT   component of the SMC5-SMC6 complex involved in DNA repair.";
RL   J. Biol. Chem. 277:21585-21591(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NSE3.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [5]
RP   SUBUNIT.
RX   PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA   Zhao X., Blobel G.;
RT   "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT   repair and chromosomal organization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
CC   -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC       damage that is distinct from classical nucleotide excision repair and
CC       in repair of ionizing radiation damage. Functions in homologous
CC       recombination repair of DNA double strand breaks and in recovery of
CC       stalled replication forks. {ECO:0000269|PubMed:11927594}.
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 of KRE29,
CC       MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6. Interacts with SMC5 and
CC       SMC6. Interacts with NSE3. {ECO:0000269|PubMed:11927594,
CC       ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:15738391}.
CC   -!- INTERACTION:
CC       Q07913; Q08204: SMC5; NbExp=5; IntAct=EBI-30144, EBI-34125;
CC       Q07913; Q12749: SMC6; NbExp=4; IntAct=EBI-30144, EBI-15099;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11927594}.
CC   -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
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DR   EMBL; Z73179; CAA97529.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09325.1; -; Genomic_DNA.
DR   PIR; S64829; S64829.
DR   RefSeq; NP_013107.1; NM_001181894.1.
DR   AlphaFoldDB; Q07913; -.
DR   SMR; Q07913; -.
DR   BioGRID; 31280; 261.
DR   ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR   DIP; DIP-8847N; -.
DR   IntAct; Q07913; 4.
DR   STRING; 4932.YLR007W; -.
DR   MaxQB; Q07913; -.
DR   PaxDb; Q07913; -.
DR   PRIDE; Q07913; -.
DR   EnsemblFungi; YLR007W_mRNA; YLR007W; YLR007W.
DR   GeneID; 850693; -.
DR   KEGG; sce:YLR007W; -.
DR   SGD; S000003997; NSE1.
DR   VEuPathDB; FungiDB:YLR007W; -.
DR   eggNOG; KOG4718; Eukaryota.
DR   GeneTree; ENSGT00390000009084; -.
DR   HOGENOM; CLU_826927_0_0_1; -.
DR   InParanoid; Q07913; -.
DR   OMA; KIIRINH; -.
DR   BioCyc; YEAST:G3O-32168-MON; -.
DR   Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR   PRO; PR:Q07913; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07913; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IDA:SGD.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0006301; P:postreplication repair; IGI:SGD.
DR   GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR   GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR   CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011513; Nse1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR014857; Znf_RING-like.
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   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..336
FT                   /note="Non-structural maintenance of chromosomes element 1"
FT                   /id="PRO_0000114116"
FT   ZN_FING         268..327
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   336 AA;  38335 MW;  43237EFB55B44042 CRC64;
     MEVHEEQVSA PVTGDATAKY LLQYILSARG ICHENALILA LMRLETDAST LNTEWSIQQW
     VDKLNDYINA INVKLNLLGY KIIRINHGIG RNAVTLKAKQ NFESFEDNTA IRAHNNDYAV
     LQSIVLPESN RFFVYVNLAS TEETKLATRF NQNEIEFMKW AIEQFMISGE TIVEGPALET
     SIIVKEVNRI LVAATGDSNL AKWRKFSTFT VGSTNLFQFQ ELTATDIEDL LLRLCELKWF
     YRTQEGKFGI DLRCIAELEE YLTSMYNLNT CQNCHKLAIQ GVRCGNESCR EENEETGENS
     LSQIWHVDCF KHYITHVSKN CDRCGSSLIT EGVYVI
 
 
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