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Database: UniProt
Entry: PSF1_YEAST
LinkDB: PSF1_YEAST
Original site: PSF1_YEAST 
ID   PSF1_YEAST              Reviewed;         208 AA.
AC   Q12488; D6VRZ9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=DNA replication complex GINS protein PSF1;
DE   AltName: Full=Partner of Sld five 1;
GN   Name=PSF1; OrderedLocusNames=YDR013W; ORFNames=PZA208, YD8119.18;
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], FUNCTION, INTERACTION WITH DPB11 AND
RP   SLD3, COMPOSITION OF THE GINS COMPLEX, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF ARG-84.
RX   PubMed=12730134; DOI=10.1101/gad.1065903;
RA   Takayama Y., Kamimura Y., Okawa M., Muramatsu S., Sugino A., Araki H.;
RT   "GINS, a novel multiprotein complex required for chromosomal DNA
RT   replication in budding yeast.";
RL   Genes Dev. 17:1153-1165(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8896275;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA   Eide L.G., Sander C., Prydz H.;
RT   "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT   IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL   Yeast 12:1085-1090(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PSF2.
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   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Required for DNA replication. Functions as part of the GINS
CC       complex which plays an essential role in the initiation of DNA
CC       replication by binding to DNA replication origins and facilitating the
CC       assembly of the DNA replication machinery. Required for the chromatin
CC       binding of CDC45. {ECO:0000269|PubMed:12730134}.
CC   -!- SUBUNIT: Component of the GINS complex which is a heterotetramer of
CC       SLD5, PSF1, PSF2 and PSF3. Interacts with PSF2.
CC       {ECO:0000269|PubMed:14690591}.
CC   -!- INTERACTION:
CC       Q12488; Q01454: CTF4; NbExp=7; IntAct=EBI-22066, EBI-5209;
CC       Q12488; P30665: MCM4; NbExp=5; IntAct=EBI-22066, EBI-4326;
CC       Q12488; P40359: PSF2; NbExp=5; IntAct=EBI-22066, EBI-25936;
CC       Q12488; Q03406: SLD5; NbExp=6; IntAct=EBI-22066, EBI-37437;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730134}.
CC       Note=Associates with autonomously replicating sequence (ARS) regions in
CC       S phase. This association requires SLD3 and DPB11.
CC   -!- MISCELLANEOUS: Present with 1431 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the GINS1/PSF1 family. {ECO:0000305}.
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DR   EMBL; X95966; CAA65205.1; -; Genomic_DNA.
DR   EMBL; Z74309; CAA98833.1; -; Genomic_DNA.
DR   EMBL; Z48008; CAA88073.1; -; Genomic_DNA.
DR   EMBL; AY557650; AAS55976.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11859.1; -; Genomic_DNA.
DR   PIR; S50994; S50994.
DR   RefSeq; NP_010296.3; NM_001180321.3.
DR   PDB; 3JC5; EM; 4.70 A; A=1-206.
DR   PDB; 3JC6; EM; 3.70 A; A=1-208.
DR   PDB; 3JC7; EM; 4.80 A; A=1-206.
DR   PDB; 5U8S; EM; 6.10 A; A=1-208.
DR   PDB; 5U8T; EM; 4.90 A; A=1-208.
DR   PDB; 6HV9; EM; 4.98 A; C=1-208.
DR   PDB; 6PTJ; EM; 3.80 A; A=1-208.
DR   PDB; 6PTN; EM; 5.80 A; A/a=1-208.
DR   PDB; 6PTO; EM; 7.00 A; A/a/n=1-208.
DR   PDB; 6SKL; EM; 3.70 A; A=1-208.
DR   PDB; 6U0M; EM; 3.90 A; A=1-208.
DR   PDB; 7PMK; EM; 3.20 A; A=1-208.
DR   PDB; 7PMN; EM; 3.20 A; A=1-208.
DR   PDB; 8B9A; EM; 3.50 A; C=1-208.
DR   PDB; 8B9B; EM; 3.50 A; C=1-208.
DR   PDB; 8B9C; EM; 4.60 A; C=1-208.
DR   PDB; 8KG6; EM; 3.07 A; A=1-208.
DR   PDB; 8KG8; EM; 4.23 A; A=1-208.
DR   PDB; 8KG9; EM; 4.52 A; A=1-208.
DR   PDB; 8W7M; EM; 4.12 A; A=1-208.
DR   PDBsum; 3JC5; -.
DR   PDBsum; 3JC6; -.
DR   PDBsum; 3JC7; -.
DR   PDBsum; 5U8S; -.
DR   PDBsum; 5U8T; -.
DR   PDBsum; 6HV9; -.
DR   PDBsum; 6PTJ; -.
DR   PDBsum; 6PTN; -.
DR   PDBsum; 6PTO; -.
DR   PDBsum; 6SKL; -.
DR   PDBsum; 6U0M; -.
DR   PDBsum; 7PMK; -.
DR   PDBsum; 7PMN; -.
DR   PDBsum; 8B9A; -.
DR   PDBsum; 8B9B; -.
DR   PDBsum; 8B9C; -.
DR   PDBsum; 8KG6; -.
DR   PDBsum; 8KG8; -.
DR   PDBsum; 8KG9; -.
DR   PDBsum; 8W7M; -.
DR   AlphaFoldDB; Q12488; -.
DR   EMDB; EMD-0288; -.
DR   EMDB; EMD-10227; -.
DR   EMDB; EMD-13537; -.
DR   EMDB; EMD-13539; -.
DR   EMDB; EMD-15924; -.
DR   EMDB; EMD-20471; -.
DR   EMDB; EMD-20472; -.
DR   EMDB; EMD-20473; -.
DR   EMDB; EMD-20607; -.
DR   EMDB; EMD-8518; -.
DR   EMDB; EMD-8519; -.
DR   SMR; Q12488; -.
DR   BioGRID; 32064; 297.
DR   ComplexPortal; CPX-1641; GINS complex.
DR   DIP; DIP-1812N; -.
DR   IntAct; Q12488; 30.
DR   MINT; Q12488; -.
DR   STRING; 4932.YDR013W; -.
DR   MaxQB; Q12488; -.
DR   PaxDb; 4932-YDR013W; -.
DR   PeptideAtlas; Q12488; -.
DR   EnsemblFungi; YDR013W_mRNA; YDR013W; YDR013W.
DR   GeneID; 851576; -.
DR   KEGG; sce:YDR013W; -.
DR   AGR; SGD:S000002420; -.
DR   SGD; S000002420; PSF1.
DR   VEuPathDB; FungiDB:YDR013W; -.
DR   eggNOG; KOG3303; Eukaryota.
DR   GeneTree; ENSGT00390000013968; -.
DR   HOGENOM; CLU_079191_0_0_1; -.
DR   InParanoid; Q12488; -.
DR   OMA; NHLCMRR; -.
DR   OrthoDB; 166901at2759; -.
DR   BioCyc; YEAST:G3O-29632-MONOMER; -.
DR   Reactome; R-SCE-176974; Unwinding of DNA.
DR   BioGRID-ORCS; 851576; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q12488; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12488; Protein.
DR   GO; GO:0071162; C:CMG complex; IDA:SGD.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IMP:SGD.
DR   GO; GO:0000811; C:GINS complex; IPI:SGD.
DR   GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR   GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IBA:GO_Central.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR   CDD; cd11710; GINS_A_psf1; 1.
DR   CDD; cd21696; GINS_B_Psf1; 1.
DR   Gene3D; 1.20.58.1030; -; 1.
DR   InterPro; IPR021151; GINS_A.
DR   InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR   InterPro; IPR005339; GINS_Psf1.
DR   PANTHER; PTHR12914:SF2; DNA REPLICATION COMPLEX GINS PROTEIN PSF1; 1.
DR   PANTHER; PTHR12914; PARTNER OF SLD5; 1.
DR   Pfam; PF05916; Sld5; 1.
DR   SUPFAM; SSF158573; GINS helical bundle-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; DNA replication; Nucleus; Reference proteome.
FT   CHAIN           1..208
FT                   /note="DNA replication complex GINS protein PSF1"
FT                   /id="PRO_0000219040"
FT   MUTAGEN         84
FT                   /note="R->G: In PSF1-1; temperature-sensitive mutant.
FT                   Defective in DNA replication. Impaired chromatin binding of
FT                   CDC45."
FT                   /evidence="ECO:0000269|PubMed:12730134"
FT   HELIX           4..21
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           34..57
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            58..66
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           67..103
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           125..143
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          161..167
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:7PMK"
FT   HELIX           197..201
FT                   /evidence="ECO:0007829|PDB:7PMK"
SQ   SEQUENCE   208 AA;  24204 MW;  4667D8152C1AB5B4 CRC64;
     MYGDLGNKLV LEAKRTKQLY ARSNQDVNLP MYHEDIIRNI LKEVSNLRKN TEYLKEQQQL
     GMLDDKVAKC QYFVTLLCME RNKRCLLAYQ RLRTDILDSM AWNNNGLDLM SSITFSQQDT
     NNLSHQEQEY LKEYCDLITD LKSGDLVDID LSGSLVPPSD VFIDVRVLKD AGEIQTEYGV
     FNLIKDSQFF VRQSDVERLI QQGYLQKI
//
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