ELG1_YEAST
ID ELG1_YEAST Reviewed; 791 AA.
AC Q12050; D6W2K2; O94148; Q03129; Q7LI57;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Telomere length regulation protein ELG1;
DE AltName: Full=Regulator of Ty1 transposition protein 110;
DE AltName: Full=Telomere elongation suppressor ELG1;
GN Name=ELG1; Synonyms=RTT110; OrderedLocusNames=YOR144C;
GN ORFNames=O3510, YOR3510C;
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 [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-183.
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [5]
RP FUNCTION, AND INTERACTION WITH RFC2; RFC3; RFC4 AND RFC5.
RX PubMed=12912927; DOI=10.1093/emboj/cdg406;
RA Bellaoui M., Chang M., Ou J., Xu H., Boone C., Brown G.W.;
RT "Elg1 forms an alternative RFC complex important for DNA replication and
RT genome integrity.";
RL EMBO J. 22:4304-4313(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH RFC2; RFC4 AND RFC5.
RX PubMed=12909721; DOI=10.1073/pnas.1633757100;
RA Ben-Aroya S., Koren A., Liefshitz B., Steinlauf R., Kupiec M.;
RT "ELG1, a yeast gene required for genome stability, forms a complex related
RT to replication factor C.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9906-9911(2003).
RN [8]
RP FUNCTION.
RX PubMed=14745004; DOI=10.1073/pnas.0307796100;
RA Smolikov S., Mazor Y., Krauskopf A.;
RT "ELG1, a regulator of genome stability, has a role in telomere length
RT regulation and in silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1656-1661(2004).
RN [9]
RP FUNCTION.
RX PubMed=13678589; DOI=10.1016/s0960-9822(03)00578-5;
RA Kanellis P., Agyei R., Durocher D.;
RT "Elg1 forms an alternative PCNA-interacting RFC complex required to
RT maintain genome stability.";
RL Curr. Biol. 13:1583-1595(2003).
RN [10]
RP IDENTIFICATION IN THE ELG1-RFC COMPLEX.
RX PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA Bylund G.O., Burgers P.M.;
RT "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT establishment complex.";
RL Mol. Cell. Biol. 25:5445-5455(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the negative control of telomere length and in
CC telomeric silencing through a replication-mediated pathway. May have a
CC role in Okazaki fragment maturation. Required for S-phase progression.
CC Component of the RFC-like ELG1-RFC complex which appears to have a role
CC in DNA replication, replication fork re-start, recombination and
CC repair. {ECO:0000269|PubMed:12909721, ECO:0000269|PubMed:12912927,
CC ECO:0000269|PubMed:13678589, ECO:0000269|PubMed:14745004}.
CC -!- SUBUNIT: Component of the ELG1-RFC complex which consists of ELG1,
CC RFC2, RFC3, RFC4 and RFC5. {ECO:0000269|PubMed:15964801}.
CC -!- INTERACTION:
CC Q12050; Q03973: HMO1; NbExp=2; IntAct=EBI-32195, EBI-33047;
CC Q12050; P15873: POL30; NbExp=9; IntAct=EBI-32195, EBI-12993;
CC Q12050; P40348: RFC2; NbExp=2; IntAct=EBI-32195, EBI-14992;
CC Q12050; P40339: RFC4; NbExp=5; IntAct=EBI-32195, EBI-15009;
CC Q12050; P38251: RFC5; NbExp=4; IntAct=EBI-32195, EBI-15016;
CC Q12050; Q12306: SMT3; NbExp=11; IntAct=EBI-32195, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC Chromosome, telomere {ECO:0000305|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the ELG1 family. {ECO:0000305}.
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DR EMBL; X94335; CAA64062.1; -; Genomic_DNA.
DR EMBL; Z75052; CAA99348.1; -; Genomic_DNA.
DR EMBL; Z75053; CAA99351.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49631.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10918.1; -; Genomic_DNA.
DR PIR; S61698; S61698.
DR RefSeq; NP_014787.3; NM_001183563.3.
DR AlphaFoldDB; Q12050; -.
DR BioGRID; 34541; 465.
DR ComplexPortal; CPX-422; ELG1-RFC complex.
DR DIP; DIP-6498N; -.
DR IntAct; Q12050; 7.
DR MINT; Q12050; -.
DR STRING; 4932.YOR144C; -.
DR iPTMnet; Q12050; -.
DR MaxQB; Q12050; -.
DR PaxDb; Q12050; -.
DR PRIDE; Q12050; -.
DR EnsemblFungi; YOR144C_mRNA; YOR144C; YOR144C.
DR GeneID; 854315; -.
DR KEGG; sce:YOR144C; -.
DR SGD; S000005670; ELG1.
DR VEuPathDB; FungiDB:YOR144C; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_019060_0_0_1; -.
DR InParanoid; Q12050; -.
DR OMA; TTHFVKN; -.
DR BioCyc; YEAST:G3O-33663-MON; -.
DR PRO; PR:Q12050; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12050; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0090618; P:DNA clamp unloading; IDA:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; Nucleus; Phosphoprotein; Reference proteome;
KW Telomere.
FT CHAIN 1..791
FT /note="Telomere length regulation protein ELG1"
FT /id="PRO_0000086954"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 791 AA; 91262 MW; 2BF86887238F83FE CRC64;
MKRHVSLSDI LTGNKRKVRR QDALQITIDD ENDTESGTFD ARTAKHDDSS VIFLNHSVVK
PIEAVSTNHK SAKEFLMTKR TKEKCDDDDD DLIVISDKSP KSETNCSKIA LSQEHEDDIS
IISTSRIKSS LLNERASKIK NFLKHETTDT FKRLNSISKL NEIEPPLPLH QSIFPVGDKE
LSDRSVDIPL PFRTIPPLNH NFLPSDYESL KDKNSASCIP VRYQAPVLLG TNIKRNTTLT
WPQLFKPVTL KQVLIEPKLK LRIKNWIETS FHTLEKPTLR NRLLNRINPN KQQGSGDELA
NFIVPDLEED ENLRPDFYRN GEANSSLSEF VPLMILHGNS IGKKTLIQTI MREIAGDDNS
YQIYEVNSNM NRSKKDLLDI LLDFTTTHYV KDSSKRKSDY GLVLFNDVDV LFKEHDRGYW
AMISKLCEFS RRPLVLTCKD LSLVPSELIA LASEQNSLFH TKKISTSTVY AFLTKYLKSL
EIEVCDDWLR DVVKQNNADI RKCLMHLQFW CVDTEADLIS SKNRLPVLTS TLGSSVKDIS
QLTDLLSIND VIGQATLNRS MVRQEIDSTT MTPEKVNTFQ DQNLDDEMKL KFDYVIDYKL
HLNDPNRQPL LPFELNIYQH IQEQLEARYS YVREANHRLD NEYLVNRFKK MTESTLNFLA
SRIPKYDHLQ SARRTRNSKK ISDILNQFKG IYNDETLNEN AEIDLLSATT QQIKAEINPF
VFEIAKSDAN VKNENKQIFE LHSENVSERR YKDLVYQLSQ EGVLKNVWFN ADPSIVVRKW
EHLHSGFSKN K
