Full text data of GINS4
GINS4
(SLD5)
[Confidence: low (only semi-automatic identification from reviews)]
DNA replication complex GINS protein SLD5 (GINS complex subunit 4; DNA replication complex GINS protein SLD5, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA replication complex GINS protein SLD5 (GINS complex subunit 4; DNA replication complex GINS protein SLD5, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRT9
ID SLD5_HUMAN Reviewed; 223 AA.
AC Q9BRT9; B2R8H5; D3DSY0; Q8N648;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=DNA replication complex GINS protein SLD5;
DE AltName: Full=GINS complex subunit 4;
DE Contains:
DE RecName: Full=DNA replication complex GINS protein SLD5, N-terminally processed;
GN Name=GINS4; Synonyms=SLD5;
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] (ISOFORM 1).
RC TISSUE=Thymus, and Tongue;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Placenta;
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 [4]
RP SUBUNIT, AND INTERACTION WITH DNA PRIMASE.
RX PubMed=17170760; DOI=10.1038/sj.embor.7400870;
RA De Falco M., Ferrari E., De Felice M., Rossi M., Hubscher U.,
RA Pisani F.M.;
RT "The human GINS complex binds to and specifically stimulates human DNA
RT polymerase alpha-primase.";
RL EMBO Rep. 8:99-103(2007).
RN [5]
RP INDUCTION.
RX PubMed=17611626; DOI=10.1371/journal.pone.0000594;
RA Ryu B., Kim D.S., Deluca A.M., Alani R.M.;
RT "Comprehensive expression profiling of tumor cell lines identifies
RT molecular signatures of melanoma progression.";
RL PLoS ONE 2:E594-E594(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-12 AND SER-16, AND 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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-12 AND SER-16, MASS SPECTROMETRY, AND CLEAVAGE
RP OF INITIATOR METHIONINE.
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 [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 11-213 IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [11]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, SUBUNIT, AND REGION.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS2
RP AND GINS3, AND SUBUNIT.
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. GINS4 is important for GINS complex assembly. GINS complex
CC seems to bind preferentially to single-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 GINS1. GINS complex interacts with DNA primase in vitro.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRT9-2; Sequence=VSP_032738, VSP_032739;
CC -!- INDUCTION: Significantly up-regulated in aggressive melanomas.
CC -!- MASS SPECTROMETRY: Mass=98373; Mass_error=13; Method=Electrospray;
CC Range=1-223; Note=This is the measured mass for the GINS complex;
CC Source=PubMed:17557111;
CC -!- SIMILARITY: Belongs to the GINS4/SLD5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK095334; BAG53029.1; -; mRNA.
DR EMBL; AK313373; BAG36172.1; -; mRNA.
DR EMBL; CH471080; EAW63256.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63257.1; -; Genomic_DNA.
DR EMBL; BC005995; AAH05995.1; -; mRNA.
DR EMBL; BC027454; AAH27454.1; -; mRNA.
DR RefSeq; NP_115712.1; NM_032336.2.
DR RefSeq; XP_005273716.1; XM_005273659.1.
DR UniGene; Hs.656996; -.
DR PDB; 2E9X; X-ray; 2.30 A; D/H=1-223.
DR PDB; 2EHO; X-ray; 3.00 A; A/E/I=11-213.
DR PDB; 2Q9Q; X-ray; 2.36 A; B/F=1-223.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR ProteinModelPortal; Q9BRT9; -.
DR SMR; Q9BRT9; 21-212.
DR DIP; DIP-29334N; -.
DR IntAct; Q9BRT9; 2.
DR MINT; MINT-1469672; -.
DR STRING; 9606.ENSP00000276533; -.
DR PhosphoSite; Q9BRT9; -.
DR DMDM; 74732928; -.
DR PaxDb; Q9BRT9; -.
DR PeptideAtlas; Q9BRT9; -.
DR PRIDE; Q9BRT9; -.
DR Ensembl; ENST00000276533; ENSP00000276533; ENSG00000147536.
DR Ensembl; ENST00000518671; ENSP00000428754; ENSG00000147536.
DR Ensembl; ENST00000520710; ENSP00000429581; ENSG00000147536.
DR GeneID; 84296; -.
DR KEGG; hsa:84296; -.
DR UCSC; uc003xnx.3; human.
DR CTD; 84296; -.
DR GeneCards; GC08P041388; -.
DR HGNC; HGNC:28226; GINS4.
DR HPA; HPA024663; -.
DR HPA; HPA026580; -.
DR MIM; 610611; gene.
DR neXtProt; NX_Q9BRT9; -.
DR PharmGKB; PA145008337; -.
DR eggNOG; COG5086; -.
DR HOGENOM; HOG000215319; -.
DR HOVERGEN; HBG059490; -.
DR InParanoid; Q9BRT9; -.
DR KO; K10735; -.
DR OMA; QLDHMEE; -.
DR PhylomeDB; Q9BRT9; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_383; DNA Replication.
DR EvolutionaryTrace; Q9BRT9; -.
DR GenomeRNAi; 84296; -.
DR NextBio; 73952; -.
DR PRO; PR:Q9BRT9; -.
DR ArrayExpress; Q9BRT9; -.
DR Bgee; Q9BRT9; -.
DR CleanEx; HS_GINS4; -.
DR Genevestigator; Q9BRT9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR008591; GINS_Sld5.
DR PANTHER; PTHR21206; PTHR21206; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF007764; Sld5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 223 DNA replication complex GINS protein
FT SLD5.
FT /FTId=PRO_0000327620.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 223 DNA replication complex GINS protein
FT SLD5, N-terminally processed.
FT /FTId=PRO_0000421794.
FT REGION 166 223 Important for GINS complex assembly.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylthreonine; in DNA replication
FT complex GINS protein SLD5, N-terminally
FT processed.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 16 16 Phosphoserine.
FT VAR_SEQ 100 100 I -> V (in isoform 2).
FT /FTId=VSP_032738.
FT VAR_SEQ 101 223 Missing (in isoform 2).
FT /FTId=VSP_032739.
FT HELIX 23 39
FT STRAND 40 42
FT HELIX 48 60
FT HELIX 72 102
FT HELIX 104 112
FT HELIX 124 144
FT HELIX 146 148
FT HELIX 151 153
FT HELIX 158 161
FT STRAND 170 177
FT STRAND 179 184
FT HELIX 190 192
FT STRAND 194 198
FT STRAND 203 207
FT HELIX 208 217
FT STRAND 218 223
SQ SEQUENCE 223 AA; 26047 MW; 8FAB619A21968BB9 CRC64;
MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH
MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS
SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE
NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI
//
ID SLD5_HUMAN Reviewed; 223 AA.
AC Q9BRT9; B2R8H5; D3DSY0; Q8N648;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=DNA replication complex GINS protein SLD5;
DE AltName: Full=GINS complex subunit 4;
DE Contains:
DE RecName: Full=DNA replication complex GINS protein SLD5, N-terminally processed;
GN Name=GINS4; Synonyms=SLD5;
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] (ISOFORM 1).
RC TISSUE=Thymus, and Tongue;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Placenta;
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 [4]
RP SUBUNIT, AND INTERACTION WITH DNA PRIMASE.
RX PubMed=17170760; DOI=10.1038/sj.embor.7400870;
RA De Falco M., Ferrari E., De Felice M., Rossi M., Hubscher U.,
RA Pisani F.M.;
RT "The human GINS complex binds to and specifically stimulates human DNA
RT polymerase alpha-primase.";
RL EMBO Rep. 8:99-103(2007).
RN [5]
RP INDUCTION.
RX PubMed=17611626; DOI=10.1371/journal.pone.0000594;
RA Ryu B., Kim D.S., Deluca A.M., Alani R.M.;
RT "Comprehensive expression profiling of tumor cell lines identifies
RT molecular signatures of melanoma progression.";
RL PLoS ONE 2:E594-E594(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-12 AND SER-16, AND 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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-12 AND SER-16, MASS SPECTROMETRY, AND CLEAVAGE
RP OF INITIATOR METHIONINE.
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 [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 11-213 IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [11]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, SUBUNIT, AND REGION.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS2
RP AND GINS3, AND SUBUNIT.
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. GINS4 is important for GINS complex assembly. GINS complex
CC seems to bind preferentially to single-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 GINS1. GINS complex interacts with DNA primase in vitro.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRT9-2; Sequence=VSP_032738, VSP_032739;
CC -!- INDUCTION: Significantly up-regulated in aggressive melanomas.
CC -!- MASS SPECTROMETRY: Mass=98373; Mass_error=13; Method=Electrospray;
CC Range=1-223; Note=This is the measured mass for the GINS complex;
CC Source=PubMed:17557111;
CC -!- SIMILARITY: Belongs to the GINS4/SLD5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK095334; BAG53029.1; -; mRNA.
DR EMBL; AK313373; BAG36172.1; -; mRNA.
DR EMBL; CH471080; EAW63256.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63257.1; -; Genomic_DNA.
DR EMBL; BC005995; AAH05995.1; -; mRNA.
DR EMBL; BC027454; AAH27454.1; -; mRNA.
DR RefSeq; NP_115712.1; NM_032336.2.
DR RefSeq; XP_005273716.1; XM_005273659.1.
DR UniGene; Hs.656996; -.
DR PDB; 2E9X; X-ray; 2.30 A; D/H=1-223.
DR PDB; 2EHO; X-ray; 3.00 A; A/E/I=11-213.
DR PDB; 2Q9Q; X-ray; 2.36 A; B/F=1-223.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR ProteinModelPortal; Q9BRT9; -.
DR SMR; Q9BRT9; 21-212.
DR DIP; DIP-29334N; -.
DR IntAct; Q9BRT9; 2.
DR MINT; MINT-1469672; -.
DR STRING; 9606.ENSP00000276533; -.
DR PhosphoSite; Q9BRT9; -.
DR DMDM; 74732928; -.
DR PaxDb; Q9BRT9; -.
DR PeptideAtlas; Q9BRT9; -.
DR PRIDE; Q9BRT9; -.
DR Ensembl; ENST00000276533; ENSP00000276533; ENSG00000147536.
DR Ensembl; ENST00000518671; ENSP00000428754; ENSG00000147536.
DR Ensembl; ENST00000520710; ENSP00000429581; ENSG00000147536.
DR GeneID; 84296; -.
DR KEGG; hsa:84296; -.
DR UCSC; uc003xnx.3; human.
DR CTD; 84296; -.
DR GeneCards; GC08P041388; -.
DR HGNC; HGNC:28226; GINS4.
DR HPA; HPA024663; -.
DR HPA; HPA026580; -.
DR MIM; 610611; gene.
DR neXtProt; NX_Q9BRT9; -.
DR PharmGKB; PA145008337; -.
DR eggNOG; COG5086; -.
DR HOGENOM; HOG000215319; -.
DR HOVERGEN; HBG059490; -.
DR InParanoid; Q9BRT9; -.
DR KO; K10735; -.
DR OMA; QLDHMEE; -.
DR PhylomeDB; Q9BRT9; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_383; DNA Replication.
DR EvolutionaryTrace; Q9BRT9; -.
DR GenomeRNAi; 84296; -.
DR NextBio; 73952; -.
DR PRO; PR:Q9BRT9; -.
DR ArrayExpress; Q9BRT9; -.
DR Bgee; Q9BRT9; -.
DR CleanEx; HS_GINS4; -.
DR Genevestigator; Q9BRT9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR008591; GINS_Sld5.
DR PANTHER; PTHR21206; PTHR21206; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF007764; Sld5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 223 DNA replication complex GINS protein
FT SLD5.
FT /FTId=PRO_0000327620.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 223 DNA replication complex GINS protein
FT SLD5, N-terminally processed.
FT /FTId=PRO_0000421794.
FT REGION 166 223 Important for GINS complex assembly.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylthreonine; in DNA replication
FT complex GINS protein SLD5, N-terminally
FT processed.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 16 16 Phosphoserine.
FT VAR_SEQ 100 100 I -> V (in isoform 2).
FT /FTId=VSP_032738.
FT VAR_SEQ 101 223 Missing (in isoform 2).
FT /FTId=VSP_032739.
FT HELIX 23 39
FT STRAND 40 42
FT HELIX 48 60
FT HELIX 72 102
FT HELIX 104 112
FT HELIX 124 144
FT HELIX 146 148
FT HELIX 151 153
FT HELIX 158 161
FT STRAND 170 177
FT STRAND 179 184
FT HELIX 190 192
FT STRAND 194 198
FT STRAND 203 207
FT HELIX 208 217
FT STRAND 218 223
SQ SEQUENCE 223 AA; 26047 MW; 8FAB619A21968BB9 CRC64;
MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH
MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS
SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE
NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI
//
MIM
610611
*RECORD*
*FIELD* NO
610611
*FIELD* TI
*610611 GINS COMPLEX SUBUNIT 4; GINS4
;;SLD5, S. CEREVISIAE, HOMOLOG OF; SLD5
*FIELD* TX
read more
DESCRIPTION
The yeast heterotetrameric GINS complex is made up of Sld5, Psf1 (GINS1;
610608), Psf2 (GINS2; 610609), and Psf3 (GINS3; 610610). The formation
of the GINS 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 SLD5,
Takayama et al. (2003) identified GINS4, which they called SLD5. The
deduced protein contains 223 amino acids.
Using mouse Psf1 as bait in a yeast 2-hybrid analysis of an 11-day mouse
embryo cDNA library, Kong et al. (2006) cloned Sld5. The deduced
223-amino acid protein contains an N-terminal coiled-coil domain, a
central basic region, and a C-terminal domain that is conserved between
the mouse and yeast proteins. RT-PCR of mouse tissues detected abundant
expression in adult testis, and weak expression in thymus and bone
marrow. No Sld5 was detected in brain, lung, liver, spleen, kidney, and
heart. Immunohistochemical analysis detected Psf1 and Sld5 in the
cytoplasm of transfected NIH3T3 mouse fibroblast.
GENE FUNCTION
By coimmunoprecipitation analysis, Kong et al. (2006) demonstrated that
mouse Sld5 and Psf1 interacted in transfected NIH3T3 cells.
MAPPING
International Radiation Hybrid Mapping Consortium mapped the GINS4 gene
to chromosome 8 (TMAP RH102031).
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. Kong, L.; Ueno, M.; Itoh, M.; Yoshioka, K.; Takakura, N.: Identification
and characterization of mouse PSF1-binding protein, SLD5. Biochem.
Biophys. Res. Commun. 339: 1204-1207, 2006.
2. 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.
3. 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
610611
*FIELD* TI
*610611 GINS COMPLEX SUBUNIT 4; GINS4
;;SLD5, S. CEREVISIAE, HOMOLOG OF; SLD5
*FIELD* TX
read more
DESCRIPTION
The yeast heterotetrameric GINS complex is made up of Sld5, Psf1 (GINS1;
610608), Psf2 (GINS2; 610609), and Psf3 (GINS3; 610610). The formation
of the GINS 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 SLD5,
Takayama et al. (2003) identified GINS4, which they called SLD5. The
deduced protein contains 223 amino acids.
Using mouse Psf1 as bait in a yeast 2-hybrid analysis of an 11-day mouse
embryo cDNA library, Kong et al. (2006) cloned Sld5. The deduced
223-amino acid protein contains an N-terminal coiled-coil domain, a
central basic region, and a C-terminal domain that is conserved between
the mouse and yeast proteins. RT-PCR of mouse tissues detected abundant
expression in adult testis, and weak expression in thymus and bone
marrow. No Sld5 was detected in brain, lung, liver, spleen, kidney, and
heart. Immunohistochemical analysis detected Psf1 and Sld5 in the
cytoplasm of transfected NIH3T3 mouse fibroblast.
GENE FUNCTION
By coimmunoprecipitation analysis, Kong et al. (2006) demonstrated that
mouse Sld5 and Psf1 interacted in transfected NIH3T3 cells.
MAPPING
International Radiation Hybrid Mapping Consortium mapped the GINS4 gene
to chromosome 8 (TMAP RH102031).
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. Kong, L.; Ueno, M.; Itoh, M.; Yoshioka, K.; Takakura, N.: Identification
and characterization of mouse PSF1-binding protein, SLD5. Biochem.
Biophys. Res. Commun. 339: 1204-1207, 2006.
2. 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.
3. 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