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Non-homologous end-joining protein 1

 NEJ1_YEAST              Reviewed;         342 AA.
Q06148; D6VYR3; Q0P6Z6; Q0P6Z7; Q0P707;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 113.
RecName: Full=Non-homologous end-joining protein 1;
Name=NEJ1; Synonyms=LIF2; OrderedLocusNames=YLR265C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-17; ILE-21;
GLU-65; ALA-105; GLN-161; GLY-204; PHE-231; GLU-249; VAL-270 AND
CYS-281.
STRAIN=DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, Y55, and
YPS128;
PubMed=16951060; DOI=10.1534/genetics.106.062166;
Liti G., Barton D.B., Louis E.J.;
"Sequence diversity, reproductive isolation and species concepts in
Saccharomyces.";
Genetics 174:839-850(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION, AND INDUCTION.
PubMed=11676923; DOI=10.1016/S0960-9822(01)00488-2;
Kegel A., Sjoestrand J.O.O., Aastroem S.U.;
"Nej1p, a cell type-specific regulator of nonhomologous end joining in
yeast.";
Curr. Biol. 11:1611-1617(2001).
[6]
FUNCTION, INTERACTION WITH LIF1, AND INDUCTION.
PubMed=11711435; DOI=10.1101/gad.206801;
Frank-Vaillant M., Marcand S.;
"NHEJ regulation by mating type is exercised through a novel protein,
Lif2p, essential to the ligase IV pathway.";
Genes Dev. 15:3005-3012(2001).
[7]
FUNCTION, AND INDUCTION.
PubMed=11740566; DOI=10.1038/414666a;
Valencia M., Bentele M., Vaze M.B., Herrmann G., Kraus E., Lee S.E.,
Schaer P., Haber J.E.;
"NEJ1 controls non-homologous end joining in Saccharomyces
cerevisiae.";
Nature 414:666-669(2001).
[8]
FUNCTION.
PubMed=11701889; DOI=10.1126/science.1065672;
Ooi S.L., Shoemaker D.D., Boeke J.D.;
"A DNA microarray-based genetic screen for nonhomologous end-joining
mutants in Saccharomyces cerevisiae.";
Science 294:2552-2556(2001).
[9]
FUNCTION.
PubMed=12399380;
Wilson T.E.;
"A genomics-based screen for yeast mutants with an altered
recombination/end-joining repair ratio.";
Genetics 162:677-688(2002).
[10]
FUNCTION.
PubMed=12769859; DOI=10.1016/S1097-2765(03)00177-1;
Liti G., Louis E.J.;
"NEJ1 prevents NHEJ-dependent telomere fusions in yeast without
telomerase.";
Mol. Cell 11:1373-1378(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
INTERACTION WITH LIF1.
PubMed=16314503; DOI=10.1128/MCB.25.24.10782-10790.2005;
Palmbos P.L., Daley J.M., Wilson T.E.;
"Mutations of the Yku80 C terminus and Xrs2 FHA domain specifically
block yeast nonhomologous end joining.";
Mol. Cell. Biol. 25:10782-10790(2005).
-!- FUNCTION: Involved in non-homologous end joining (NHEJ).
Facilitates the transport of LIF1 into the nucleus, where it can
interact with DNA ligase DNL4 to repair double-strand breaks
(DSB). Mediates mating-type regulation of NHEJ. Prevents
chromosome circularisation by NHEJ in absence of telomerase.
{ECO:0000269|PubMed:11676923, ECO:0000269|PubMed:11701889,
ECO:0000269|PubMed:11711435, ECO:0000269|PubMed:11740566,
ECO:0000269|PubMed:12399380, ECO:0000269|PubMed:12769859}.
-!- INTERACTION:
P53150:LIF1; NbExp=4; IntAct=EBI-34047, EBI-23865;
P12954:SRS2; NbExp=3; IntAct=EBI-34047, EBI-18110;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus membrane {ECO:0000269|PubMed:14562095}; Multi-pass
membrane protein {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: Repressed in diploid cells.
{ECO:0000269|PubMed:11676923, ECO:0000269|PubMed:11711435,
ECO:0000269|PubMed:11740566}.
-!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the XLF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM296374; CAL35943.1; -; Genomic_DNA.
EMBL; AM296375; CAL35942.1; -; Genomic_DNA.
EMBL; AM296376; CAL35941.1; -; Genomic_DNA.
EMBL; AM296377; CAL35940.1; -; Genomic_DNA.
EMBL; AM296378; CAL35939.1; -; Genomic_DNA.
EMBL; AM296379; CAL35938.1; -; Genomic_DNA.
EMBL; AM296380; CAL35937.1; -; Genomic_DNA.
EMBL; AM296381; CAL35936.1; -; Genomic_DNA.
EMBL; AM296382; CAL36078.1; -; Genomic_DNA.
EMBL; AM296383; CAL35935.1; -; Genomic_DNA.
EMBL; AM296384; CAL35934.1; -; Genomic_DNA.
EMBL; AM296385; CAL35933.1; -; Genomic_DNA.
EMBL; AM296386; CAL35932.1; -; Genomic_DNA.
EMBL; U17244; AAB67382.1; -; Genomic_DNA.
EMBL; AY557954; AAS56280.1; -; Genomic_DNA.
EMBL; BK006945; DAA09579.1; -; Genomic_DNA.
PIR; S51402; S51402.
RefSeq; NP_013367.1; NM_001182152.1.
ProteinModelPortal; Q06148; -.
SMR; Q06148; -.
BioGrid; 31533; 107.
DIP; DIP-4776N; -.
IntAct; Q06148; 3.
MINT; Q06148; -.
STRING; 4932.YLR265C; -.
CarbonylDB; Q06148; -.
iPTMnet; Q06148; -.
MaxQB; Q06148; -.
PaxDb; Q06148; -.
PRIDE; Q06148; -.
EnsemblFungi; YLR265C; YLR265C; YLR265C.
GeneID; 850970; -.
KEGG; sce:YLR265C; -.
EuPathDB; FungiDB:YLR265C; -.
SGD; S000004255; NEJ1.
InParanoid; Q06148; -.
KO; K10983; -.
OrthoDB; EOG092C3825; -.
BioCyc; YEAST:G3O-32365-MONOMER; -.
PRO; PR:Q06148; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032807; C:DNA ligase IV complex; IPI:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0070419; C:nonhomologous end joining complex; IBA:GO_Central.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0045027; F:DNA end binding; IDA:SGD.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:0045002; P:double-strand break repair via single-strand annealing; IMP:SGD.
InterPro; IPR015381; XLF_fam.
Pfam; PF09302; XLF; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Membrane;
Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 342 Non-homologous end-joining protein 1.
/FTId=PRO_0000268689.
TRANSMEM 27 47 Helical. {ECO:0000255}.
TRANSMEM 129 149 Helical. {ECO:0000255}.
VARIANT 17 17 V -> I (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6044,
DBVPG6763, DBVPG6765, SK1, Y55 and
YPS128). {ECO:0000269|PubMed:16951060}.
VARIANT 21 21 N -> I (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
VARIANT 65 65 Q -> E (in strain: YPS128).
{ECO:0000269|PubMed:16951060}.
VARIANT 105 105 V -> A (in strain: YPS128).
{ECO:0000269|PubMed:16951060}.
VARIANT 161 161 E -> Q (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
VARIANT 204 204 D -> G (in strain: DBVPG6044 and Y55).
{ECO:0000269|PubMed:16951060}.
VARIANT 231 231 L -> F (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
VARIANT 249 249 K -> E (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
VARIANT 270 270 A -> V (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
VARIANT 281 281 R -> C (in strain: DBVPG1135, DBVPG1373,
DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6763,
DBVPG6765 and SK1).
{ECO:0000269|PubMed:16951060}.
SEQUENCE 342 AA; 39116 MW; 5E09B5F851CF03B9 CRC64;
MDSELKGQQL SDAEWCVKKI NGEGNCLLLF LPMSSPTTIV MIVLVSLERL VPYVFKLSQT
QLSQQCQSQG FTDSISLNLI KLKLMDILQA PQEINQIGLV DSNLVFSFDV SADITVSINS
VPSHVTKDMF YMILQSLCML LLKLVNLSTQ YHYVQRDILN EKQKCLDFLL ISLRDLDGGS
KVISQWAPEN SKNYESLQQC TDDDIIKKLL HKGKFQHQEF LADSLKTLLS LRNKFQDVSR
FEESGELNKK ERVRFPAVNH FYNDDFELQA DPTNEARPNS RGKIKPKTDF KPKSRESSTS
SQLRLENFSE SEATPEKTKS SSSLVEEYPQ KKRKFGKVRI KN


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