PSF2_MOUSE
ID PSF2_MOUSE Reviewed; 185 AA.
AC Q9D600; Q8BMT2;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA replication complex GINS protein PSF2;
DE AltName: Full=GINS complex subunit 2;
GN Name=Gins2; Synonyms=Psf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The GINS complex plays an essential role in the initiation of
CC DNA replication, and progression of DNA replication forks. GINS complex
CC seems to bind preferentially to single-stranded DNA.
CC {ECO:0000250|UniProtKB:Q9Y248}.
CC -!- SUBUNIT: Component of the GINS complex which is a heterotetramer of
CC GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS3.
CC GINS complex interacts with DNA primase in vitro (By similarity).
CC Component of the CMG helicase complex, composed of the MCM2-7 complex,
CC the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:Q7ZT46, ECO:0000250|UniProtKB:Q9Y248}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7ZT46}.
CC Chromosome {ECO:0000250|UniProtKB:Q7ZT46}. Note=Associates with
CC chromatin. {ECO:0000250|UniProtKB:Q7ZT46}.
CC -!- SIMILARITY: Belongs to the GINS2/PSF2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK014776; BAB29546.1; -; mRNA.
DR EMBL; AK028375; BAC25914.1; -; mRNA.
DR EMBL; AK030758; BAC27124.1; -; mRNA.
DR EMBL; BC082565; AAH82565.1; -; mRNA.
DR CCDS; CCDS40496.1; -.
DR RefSeq; NP_849187.1; NM_178856.1.
DR AlphaFoldDB; Q9D600; -.
DR SMR; Q9D600; -.
DR BioGRID; 234876; 2.
DR ComplexPortal; CPX-4502; GINS complex.
DR IntAct; Q9D600; 1.
DR MINT; Q9D600; -.
DR STRING; 10090.ENSMUSP00000034278; -.
DR iPTMnet; Q9D600; -.
DR PhosphoSitePlus; Q9D600; -.
DR EPD; Q9D600; -.
DR MaxQB; Q9D600; -.
DR PaxDb; Q9D600; -.
DR PeptideAtlas; Q9D600; -.
DR PRIDE; Q9D600; -.
DR ProteomicsDB; 291658; -.
DR Antibodypedia; 30642; 225 antibodies from 26 providers.
DR Ensembl; ENSMUST00000034278; ENSMUSP00000034278; ENSMUSG00000031821.
DR GeneID; 272551; -.
DR KEGG; mmu:272551; -.
DR UCSC; uc009nrd.1; mouse.
DR CTD; 51659; -.
DR MGI; MGI:1921019; Gins2.
DR VEuPathDB; HostDB:ENSMUSG00000031821; -.
DR eggNOG; KOG4071; Eukaryota.
DR GeneTree; ENSGT00390000007838; -.
DR HOGENOM; CLU_078274_2_0_1; -.
DR InParanoid; Q9D600; -.
DR OMA; PYHWLEL; -.
DR OrthoDB; 1382842at2759; -.
DR PhylomeDB; Q9D600; -.
DR TreeFam; TF314359; -.
DR Reactome; R-MMU-176974; Unwinding of DNA.
DR BioGRID-ORCS; 272551; 28 hits in 105 CRISPR screens.
DR ChiTaRS; Gins2; mouse.
DR PRO; PR:Q9D600; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D600; protein.
DR Bgee; ENSMUSG00000031821; Expressed in yolk sac and 151 other tissues.
DR Genevisible; Q9D600; MM.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0000811; C:GINS complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1903934; P:positive regulation of DNA primase activity; ISO:MGI.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISO:MGI.
DR InterPro; IPR021151; GINS_A.
DR InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR InterPro; IPR007257; GINS_Psf2.
DR PANTHER; PTHR12772; PTHR12772; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF028998; GINS_Psf2_subgr; 1.
DR SUPFAM; SSF158573; SSF158573; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA replication; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..185
FT /note="DNA replication complex GINS protein PSF2"
FT /id="PRO_0000194814"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y248"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y248"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y248"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y248"
FT CONFLICT 28
FT /note="L -> P (in Ref. 1; BAC25914)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="L -> M (in Ref. 1; BAC25914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21236 MW; 4DA756C71BD6EF1B CRC64;
MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVDVPLWLAI NLKQRQKCRL
LPPEWMDVEK LEQMRDEERK EETFTPVPSP HYMEITKLLL NHASDNIPKA DTIRTLIKDL
WDTRMAKLRV SADSFVRQQE AHAKLDNLTL MEISSSGAFL TQALNHMYKL RTNLQPSEST
QSQDF
