Full text data of GINS2
GINS2
(PSF2)
[Confidence: low (only semi-automatic identification from reviews)]
DNA replication complex GINS protein PSF2 (GINS complex subunit 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA replication complex GINS protein PSF2 (GINS complex subunit 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y248
ID PSF2_HUMAN Reviewed; 185 AA.
AC Q9Y248; D3DUM5; Q6IAG9;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=DNA replication complex GINS protein PSF2;
DE AltName: Full=GINS complex subunit 2;
GN Name=GINS2; Synonyms=PSF2; ORFNames=CGI-122, DC5, HSPC037;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Li Y., Peng Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-182, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH PSF1;
RP PSF3 AND GINS4, SUBUNIT, AND MASS SPECTROMETRY OF GINS COMPLEX.
RX PubMed=17557111; DOI=10.1038/sj.embor.7401002;
RA Boskovic J., Coloma J., Aparicio T., Zhou M., Robinson C.V.,
RA Mendez J., Montoya G.;
RT "Molecular architecture of the human GINS complex.";
RL EMBO Rep. 8:678-684(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND
RP GINS4, AND SUBUNIT.
RX PubMed=17545466; DOI=10.1101/gad.1548107;
RA Choi J.M., Lim H.S., Kim J.J., Song O.K., Cho Y.;
RT "Crystal structure of the human GINS complex.";
RL Genes Dev. 21:1316-1321(2007).
RN [17]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS3 AND GINS4, AND SUBUNIT.
RX PubMed=17417653; DOI=10.1038/nsmb1231;
RA Kamada K., Kubota Y., Arata T., Shindo Y., Hanaoka F.;
RT "Structure of the human GINS complex and its assembly and functional
RT interface in replication initiation.";
RL Nat. Struct. Mol. Biol. 14:388-396(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3
RP AND GINS4, SUBUNIT, AND REGION.
RX PubMed=17652513; DOI=10.1073/pnas.0705558104;
RA Chang Y.P., Wang G., Bermudez V., Hurwitz J., Chen X.S.;
RT "Crystal structure of the GINS complex and functional insights into
RT its role in DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12685-12690(2007).
CC -!- FUNCTION: The GINS complex plays an essential role in the
CC initiation of DNA replication, and progression of DNA replication
CC forks. GINS complex seems to bind preferentially to single-
CC stranded DNA.
CC -!- SUBUNIT: Component of the GINS complex which is a heterotetramer
CC of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with
CC GINS3. GINS complex interacts with DNA primase in vitro.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-747491, EBI-1180783;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- MASS SPECTROMETRY: Mass=98373; Mass_error=13; Method=Electrospray;
CC Range=1-185; Note=This is the measured mass for the GINS complex;
CC Source=PubMed:17557111;
CC -!- SIMILARITY: Belongs to the GINS2/PSF2 family.
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DR EMBL; AF125098; AAD39915.1; -; mRNA.
DR EMBL; AF151880; AAD34117.1; -; mRNA.
DR EMBL; AF201939; AAF86875.1; -; mRNA.
DR EMBL; AK001275; BAA91595.1; -; mRNA.
DR EMBL; CR457186; CAG33467.1; -; mRNA.
DR EMBL; CH471114; EAW95443.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95444.1; -; Genomic_DNA.
DR EMBL; BC003186; AAH03186.1; -; mRNA.
DR EMBL; BC010164; AAH10164.1; -; mRNA.
DR EMBL; BC062444; AAH62444.1; -; mRNA.
DR RefSeq; NP_057179.1; NM_016095.2.
DR UniGene; Hs.433180; -.
DR PDB; 2E9X; X-ray; 2.30 A; B/F=1-185.
DR PDB; 2EHO; X-ray; 3.00 A; C/G/K=1-185.
DR PDB; 2Q9Q; X-ray; 2.36 A; A/E=1-185.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR ProteinModelPortal; Q9Y248; -.
DR SMR; Q9Y248; 1-175.
DR DIP; DIP-29332N; -.
DR IntAct; Q9Y248; 3.
DR MINT; MINT-1469655; -.
DR STRING; 9606.ENSP00000253462; -.
DR PhosphoSite; Q9Y248; -.
DR DMDM; 37999822; -.
DR PaxDb; Q9Y248; -.
DR PRIDE; Q9Y248; -.
DR DNASU; 51659; -.
DR Ensembl; ENST00000253462; ENSP00000253462; ENSG00000131153.
DR GeneID; 51659; -.
DR KEGG; hsa:51659; -.
DR UCSC; uc002fja.3; human.
DR CTD; 51659; -.
DR GeneCards; GC16M085709; -.
DR HGNC; HGNC:24575; GINS2.
DR MIM; 610609; gene.
DR neXtProt; NX_Q9Y248; -.
DR PharmGKB; PA145008313; -.
DR eggNOG; COG5093; -.
DR HOGENOM; HOG000246603; -.
DR HOVERGEN; HBG044983; -.
DR InParanoid; Q9Y248; -.
DR KO; K10733; -.
DR OMA; VPPEWME; -.
DR OrthoDB; EOG7GQXXJ; -.
DR PhylomeDB; Q9Y248; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_383; DNA Replication.
DR ChiTaRS; GINS2; human.
DR EvolutionaryTrace; Q9Y248; -.
DR GeneWiki; GINS2; -.
DR GenomeRNAi; 51659; -.
DR NextBio; 55634; -.
DR PRO; PR:Q9Y248; -.
DR ArrayExpress; Q9Y248; -.
DR Bgee; Q9Y248; -.
DR CleanEx; HS_GINS2; -.
DR Genevestigator; Q9Y248; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR InterPro; IPR021151; GINS_complex.
DR InterPro; IPR007257; GINS_Psf2.
DR InterPro; IPR016906; GINS_Psf2_subgr.
DR PANTHER; PTHR12772; PTHR12772; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF028998; GINS_Psf2_subgr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; DNA replication;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1 185 DNA replication complex GINS protein
FT PSF2.
FT /FTId=PRO_0000194813.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 180 180 Phosphothreonine.
FT MOD_RES 182 182 Phosphoserine.
FT HELIX 3 10
FT STRAND 13 21
FT STRAND 26 28
FT STRAND 31 33
FT STRAND 42 45
FT HELIX 46 54
FT STRAND 57 60
FT HELIX 68 80
FT STRAND 81 83
FT HELIX 92 103
FT HELIX 104 106
FT STRAND 107 109
FT HELIX 110 137
FT STRAND 141 144
FT HELIX 150 170
FT TURN 172 174
SQ SEQUENCE 185 AA; 21428 MW; 4F6A18B1ED76F93C CRC64;
MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI NLKQRQKCRL
LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL NHASDNIPKA DEIRTLVKDM
WDTRIAKLRV SADSFVRQQE AHAKLDNLTL MEINTSGTFL TQALNHMYKL RTNLQPLEST
QSQDF
//
ID PSF2_HUMAN Reviewed; 185 AA.
AC Q9Y248; D3DUM5; Q6IAG9;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=DNA replication complex GINS protein PSF2;
DE AltName: Full=GINS complex subunit 2;
GN Name=GINS2; Synonyms=PSF2; ORFNames=CGI-122, DC5, HSPC037;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Li Y., Peng Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-182, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH PSF1;
RP PSF3 AND GINS4, SUBUNIT, AND MASS SPECTROMETRY OF GINS COMPLEX.
RX PubMed=17557111; DOI=10.1038/sj.embor.7401002;
RA Boskovic J., Coloma J., Aparicio T., Zhou M., Robinson C.V.,
RA Mendez J., Montoya G.;
RT "Molecular architecture of the human GINS complex.";
RL EMBO Rep. 8:678-684(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND
RP GINS4, AND SUBUNIT.
RX PubMed=17545466; DOI=10.1101/gad.1548107;
RA Choi J.M., Lim H.S., Kim J.J., Song O.K., Cho Y.;
RT "Crystal structure of the human GINS complex.";
RL Genes Dev. 21:1316-1321(2007).
RN [17]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS3 AND GINS4, AND SUBUNIT.
RX PubMed=17417653; DOI=10.1038/nsmb1231;
RA Kamada K., Kubota Y., Arata T., Shindo Y., Hanaoka F.;
RT "Structure of the human GINS complex and its assembly and functional
RT interface in replication initiation.";
RL Nat. Struct. Mol. Biol. 14:388-396(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3
RP AND GINS4, SUBUNIT, AND REGION.
RX PubMed=17652513; DOI=10.1073/pnas.0705558104;
RA Chang Y.P., Wang G., Bermudez V., Hurwitz J., Chen X.S.;
RT "Crystal structure of the GINS complex and functional insights into
RT its role in DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12685-12690(2007).
CC -!- FUNCTION: The GINS complex plays an essential role in the
CC initiation of DNA replication, and progression of DNA replication
CC forks. GINS complex seems to bind preferentially to single-
CC stranded DNA.
CC -!- SUBUNIT: Component of the GINS complex which is a heterotetramer
CC of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with
CC GINS3. GINS complex interacts with DNA primase in vitro.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-747491, EBI-1180783;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- MASS SPECTROMETRY: Mass=98373; Mass_error=13; Method=Electrospray;
CC Range=1-185; Note=This is the measured mass for the GINS complex;
CC Source=PubMed:17557111;
CC -!- SIMILARITY: Belongs to the GINS2/PSF2 family.
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DR EMBL; AF125098; AAD39915.1; -; mRNA.
DR EMBL; AF151880; AAD34117.1; -; mRNA.
DR EMBL; AF201939; AAF86875.1; -; mRNA.
DR EMBL; AK001275; BAA91595.1; -; mRNA.
DR EMBL; CR457186; CAG33467.1; -; mRNA.
DR EMBL; CH471114; EAW95443.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95444.1; -; Genomic_DNA.
DR EMBL; BC003186; AAH03186.1; -; mRNA.
DR EMBL; BC010164; AAH10164.1; -; mRNA.
DR EMBL; BC062444; AAH62444.1; -; mRNA.
DR RefSeq; NP_057179.1; NM_016095.2.
DR UniGene; Hs.433180; -.
DR PDB; 2E9X; X-ray; 2.30 A; B/F=1-185.
DR PDB; 2EHO; X-ray; 3.00 A; C/G/K=1-185.
DR PDB; 2Q9Q; X-ray; 2.36 A; A/E=1-185.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR ProteinModelPortal; Q9Y248; -.
DR SMR; Q9Y248; 1-175.
DR DIP; DIP-29332N; -.
DR IntAct; Q9Y248; 3.
DR MINT; MINT-1469655; -.
DR STRING; 9606.ENSP00000253462; -.
DR PhosphoSite; Q9Y248; -.
DR DMDM; 37999822; -.
DR PaxDb; Q9Y248; -.
DR PRIDE; Q9Y248; -.
DR DNASU; 51659; -.
DR Ensembl; ENST00000253462; ENSP00000253462; ENSG00000131153.
DR GeneID; 51659; -.
DR KEGG; hsa:51659; -.
DR UCSC; uc002fja.3; human.
DR CTD; 51659; -.
DR GeneCards; GC16M085709; -.
DR HGNC; HGNC:24575; GINS2.
DR MIM; 610609; gene.
DR neXtProt; NX_Q9Y248; -.
DR PharmGKB; PA145008313; -.
DR eggNOG; COG5093; -.
DR HOGENOM; HOG000246603; -.
DR HOVERGEN; HBG044983; -.
DR InParanoid; Q9Y248; -.
DR KO; K10733; -.
DR OMA; VPPEWME; -.
DR OrthoDB; EOG7GQXXJ; -.
DR PhylomeDB; Q9Y248; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_383; DNA Replication.
DR ChiTaRS; GINS2; human.
DR EvolutionaryTrace; Q9Y248; -.
DR GeneWiki; GINS2; -.
DR GenomeRNAi; 51659; -.
DR NextBio; 55634; -.
DR PRO; PR:Q9Y248; -.
DR ArrayExpress; Q9Y248; -.
DR Bgee; Q9Y248; -.
DR CleanEx; HS_GINS2; -.
DR Genevestigator; Q9Y248; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR InterPro; IPR021151; GINS_complex.
DR InterPro; IPR007257; GINS_Psf2.
DR InterPro; IPR016906; GINS_Psf2_subgr.
DR PANTHER; PTHR12772; PTHR12772; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF028998; GINS_Psf2_subgr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; DNA replication;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1 185 DNA replication complex GINS protein
FT PSF2.
FT /FTId=PRO_0000194813.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 180 180 Phosphothreonine.
FT MOD_RES 182 182 Phosphoserine.
FT HELIX 3 10
FT STRAND 13 21
FT STRAND 26 28
FT STRAND 31 33
FT STRAND 42 45
FT HELIX 46 54
FT STRAND 57 60
FT HELIX 68 80
FT STRAND 81 83
FT HELIX 92 103
FT HELIX 104 106
FT STRAND 107 109
FT HELIX 110 137
FT STRAND 141 144
FT HELIX 150 170
FT TURN 172 174
SQ SEQUENCE 185 AA; 21428 MW; 4F6A18B1ED76F93C CRC64;
MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI NLKQRQKCRL
LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL NHASDNIPKA DEIRTLVKDM
WDTRIAKLRV SADSFVRQQE AHAKLDNLTL MEINTSGTFL TQALNHMYKL RTNLQPLEST
QSQDF
//
MIM
610609
*RECORD*
*FIELD* NO
610609
*FIELD* TI
*610609 GINS COMPLEX SUBUNIT 2; GINS2
;;PSF2, S. CEREVISIAE, HOMOLOG OF; PSF2
*FIELD* TX
read more
DESCRIPTION
The yeast heterotetrameric GINS complex is made up of Sld5 (GINS4;
610611), Psf1 (GINS1; 610608), Psf2, and Psf3 (GINS3; 610610). The
formation of this complex is essential for the initiation of DNA
replication in yeast and Xenopus egg extracts (Ueno et al., 2005). See
GINS1 for additional information about the GINS complex.
CLONING
By searching a human database for sequences similar to yeast Psf2,
Takayama et al. (2003) identified GINS2, which they called PSF2. The
deduced protein contains 185 amino acids.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GINS2
gene to chromosome 16 (TMAP STS-W81647).
NOMENCLATURE
The GINS complex derives its name from the Japanese words Go, Ichi, Nii,
and San, which mean 5, 1, 2, and 3, respectively, and refer to the
numbering of the yeast homologs of the GINS complex (Takayama et al.,
2003).
*FIELD* RF
1. Takayama, Y.; Kamimura, Y.; Okawa, M.; Muramatsu, S.; Sugino, A.;
Araki, H.: GINS, a novel multiprotein complex required for chromosomal
DNA replication in budding yeast. Genes Dev. 17: 1153-1165, 2003.
2. Ueno, M.; Itoh, M.; Kong, L.; Sugihara, K.; Asano, M.; Takakura,
N.: PSF1 is essential for early embryogenesis in mice. Molec. Cell
Biol. 25: 10528-10532, 2005.
*FIELD* CD
Patricia A. Hartz: 11/29/2006
*FIELD* ED
wwang: 12/04/2006
wwang: 11/29/2006
*RECORD*
*FIELD* NO
610609
*FIELD* TI
*610609 GINS COMPLEX SUBUNIT 2; GINS2
;;PSF2, S. CEREVISIAE, HOMOLOG OF; PSF2
*FIELD* TX
read more
DESCRIPTION
The yeast heterotetrameric GINS complex is made up of Sld5 (GINS4;
610611), Psf1 (GINS1; 610608), Psf2, and Psf3 (GINS3; 610610). The
formation of this complex is essential for the initiation of DNA
replication in yeast and Xenopus egg extracts (Ueno et al., 2005). See
GINS1 for additional information about the GINS complex.
CLONING
By searching a human database for sequences similar to yeast Psf2,
Takayama et al. (2003) identified GINS2, which they called PSF2. The
deduced protein contains 185 amino acids.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GINS2
gene to chromosome 16 (TMAP STS-W81647).
NOMENCLATURE
The GINS complex derives its name from the Japanese words Go, Ichi, Nii,
and San, which mean 5, 1, 2, and 3, respectively, and refer to the
numbering of the yeast homologs of the GINS complex (Takayama et al.,
2003).
*FIELD* RF
1. Takayama, Y.; Kamimura, Y.; Okawa, M.; Muramatsu, S.; Sugino, A.;
Araki, H.: GINS, a novel multiprotein complex required for chromosomal
DNA replication in budding yeast. Genes Dev. 17: 1153-1165, 2003.
2. Ueno, M.; Itoh, M.; Kong, L.; Sugihara, K.; Asano, M.; Takakura,
N.: PSF1 is essential for early embryogenesis in mice. Molec. Cell
Biol. 25: 10528-10532, 2005.
*FIELD* CD
Patricia A. Hartz: 11/29/2006
*FIELD* ED
wwang: 12/04/2006
wwang: 11/29/2006