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Protein

DNA replication complex GINS protein PSF2

Gene

GINS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

ReactomeiREACT_6776. Unwinding of DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication complex GINS protein PSF2
Alternative name(s):
GINS complex subunit 2
Gene namesi
Name:GINS2
Synonyms:PSF2
ORF Names:CGI-122, DC5, HSPC037
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:24575. GINS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145008313.

Polymorphism and mutation databases

BioMutaiGINS2.
DMDMi37999822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185DNA replication complex GINS protein PSF2PRO_0000194813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei180 – 1801Phosphothreonine1 Publication
Modified residuei182 – 1821Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y248.
PaxDbiQ9Y248.
PRIDEiQ9Y248.

PTM databases

PhosphoSiteiQ9Y248.

Expressioni

Gene expression databases

BgeeiQ9Y248.
CleanExiHS_GINS2.
ExpressionAtlasiQ9Y248. baseline and differential.
GenevisibleiQ9Y248. HS.

Organism-specific databases

HPAiHPA057285.

Interactioni

Subunit structurei

Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS3. GINS complex interacts with DNA primase in vitro.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK2O960172EBI-747491,EBI-1180783
GINS4Q9BRT94EBI-747491,EBI-747500
MCMBPQ9BTE32EBI-747491,EBI-749378

Protein-protein interaction databases

BioGridi119664. 20 interactions.
DIPiDIP-29332N.
IntActiQ9Y248. 3 interactions.
MINTiMINT-1469655.
STRINGi9606.ENSP00000253462.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Beta strandi13 – 219Combined sources
Beta strandi26 – 283Combined sources
Beta strandi31 – 333Combined sources
Beta strandi42 – 454Combined sources
Helixi46 – 549Combined sources
Beta strandi57 – 604Combined sources
Helixi68 – 8013Combined sources
Beta strandi81 – 833Combined sources
Helixi92 – 10312Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1093Combined sources
Helixi110 – 13728Combined sources
Beta strandi141 – 1444Combined sources
Helixi150 – 17021Combined sources
Turni172 – 1743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9XX-ray2.30B/F1-185[»]
2EHOX-ray3.00C/G/K1-185[»]
2Q9QX-ray2.36A/E1-185[»]
ProteinModelPortaliQ9Y248.
SMRiQ9Y248. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y248.

Family & Domainsi

Sequence similaritiesi

Belongs to the GINS2/PSF2 family.Curated

Phylogenomic databases

eggNOGiCOG5093.
GeneTreeiENSGT00390000007838.
HOGENOMiHOG000246603.
HOVERGENiHBG044983.
InParanoidiQ9Y248.
KOiK10733.
OMAiPLWMATH.
OrthoDBiEOG7GQXXJ.
PhylomeDBiQ9Y248.
TreeFamiTF314359.

Family and domain databases

InterProiIPR021151. GINS_complex.
IPR007257. GINS_Psf2.
[Graphical view]
PANTHERiPTHR12772. PTHR12772. 1 hit.
PfamiPF05916. Sld5. 1 hit.
[Graphical view]
PIRSFiPIRSF028998. GINS_Psf2_subgr. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI
60 70 80 90 100
NLKQRQKCRL LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL
110 120 130 140 150
NHASDNIPKA DEIRTLVKDM WDTRIAKLRV SADSFVRQQE AHAKLDNLTL
160 170 180
MEINTSGTFL TQALNHMYKL RTNLQPLEST QSQDF
Length:185
Mass (Da):21,428
Last modified:November 1, 1999 - v1
Checksum:i4F6A18B1ED76F93C
GO

Mass spectrometryi

Molecular mass is 98373±13 Da from positions 1 - 185. Determined by ESI. This is the measured mass for the GINS complex.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125098 mRNA. Translation: AAD39915.1.
AF151880 mRNA. Translation: AAD34117.1.
AF201939 mRNA. Translation: AAF86875.1.
AK001275 mRNA. Translation: BAA91595.1.
CR457186 mRNA. Translation: CAG33467.1.
CH471114 Genomic DNA. Translation: EAW95443.1.
CH471114 Genomic DNA. Translation: EAW95444.1.
BC003186 mRNA. Translation: AAH03186.1.
BC010164 mRNA. Translation: AAH10164.1.
BC062444 mRNA. Translation: AAH62444.1.
CCDSiCCDS10953.1.
RefSeqiNP_057179.1. NM_016095.2.
UniGeneiHs.433180.

Genome annotation databases

EnsembliENST00000253462; ENSP00000253462; ENSG00000131153.
GeneIDi51659.
KEGGihsa:51659.
UCSCiuc002fja.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125098 mRNA. Translation: AAD39915.1.
AF151880 mRNA. Translation: AAD34117.1.
AF201939 mRNA. Translation: AAF86875.1.
AK001275 mRNA. Translation: BAA91595.1.
CR457186 mRNA. Translation: CAG33467.1.
CH471114 Genomic DNA. Translation: EAW95443.1.
CH471114 Genomic DNA. Translation: EAW95444.1.
BC003186 mRNA. Translation: AAH03186.1.
BC010164 mRNA. Translation: AAH10164.1.
BC062444 mRNA. Translation: AAH62444.1.
CCDSiCCDS10953.1.
RefSeqiNP_057179.1. NM_016095.2.
UniGeneiHs.433180.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9XX-ray2.30B/F1-185[»]
2EHOX-ray3.00C/G/K1-185[»]
2Q9QX-ray2.36A/E1-185[»]
ProteinModelPortaliQ9Y248.
SMRiQ9Y248. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119664. 20 interactions.
DIPiDIP-29332N.
IntActiQ9Y248. 3 interactions.
MINTiMINT-1469655.
STRINGi9606.ENSP00000253462.

PTM databases

PhosphoSiteiQ9Y248.

Polymorphism and mutation databases

BioMutaiGINS2.
DMDMi37999822.

Proteomic databases

MaxQBiQ9Y248.
PaxDbiQ9Y248.
PRIDEiQ9Y248.

Protocols and materials databases

DNASUi51659.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253462; ENSP00000253462; ENSG00000131153.
GeneIDi51659.
KEGGihsa:51659.
UCSCiuc002fja.3. human.

Organism-specific databases

CTDi51659.
GeneCardsiGC16M085709.
HGNCiHGNC:24575. GINS2.
HPAiHPA057285.
MIMi610609. gene.
neXtProtiNX_Q9Y248.
PharmGKBiPA145008313.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5093.
GeneTreeiENSGT00390000007838.
HOGENOMiHOG000246603.
HOVERGENiHBG044983.
InParanoidiQ9Y248.
KOiK10733.
OMAiPLWMATH.
OrthoDBiEOG7GQXXJ.
PhylomeDBiQ9Y248.
TreeFamiTF314359.

Enzyme and pathway databases

ReactomeiREACT_6776. Unwinding of DNA.

Miscellaneous databases

ChiTaRSiGINS2. human.
EvolutionaryTraceiQ9Y248.
GeneWikiiGINS2.
GenomeRNAii51659.
NextBioi55634.
PROiQ9Y248.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y248.
CleanExiHS_GINS2.
ExpressionAtlasiQ9Y248. baseline and differential.
GenevisibleiQ9Y248. HS.

Family and domain databases

InterProiIPR021151. GINS_complex.
IPR007257. GINS_Psf2.
[Graphical view]
PANTHERiPTHR12772. PTHR12772. 1 hit.
PfamiPF05916. Sld5. 1 hit.
[Graphical view]
PIRSFiPIRSF028998. GINS_Psf2_subgr. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Novel genes expressed in human dendritic cells."
    Li Y., Peng Y., Li N., Gu W., Han Z., Fu G., Chen Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Dendritic cell.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH PSF1; PSF3 AND GINS4, SUBUNIT, MASS SPECTROMETRY OF GINS COMPLEX.
  16. "Crystal structure of the human GINS complex."
    Choi J.M., Lim H.S., Kim J.J., Song O.K., Cho Y.
    Genes Dev. 21:1316-1321(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND GINS4, SUBUNIT.
  17. "Structure of the human GINS complex and its assembly and functional interface in replication initiation."
    Kamada K., Kubota Y., Arata T., Shindo Y., Hanaoka F.
    Nat. Struct. Mol. Biol. 14:388-396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND GINS4, SUBUNIT.
  18. "Crystal structure of the GINS complex and functional insights into its role in DNA replication."
    Chang Y.P., Wang G., Bermudez V., Hurwitz J., Chen X.S.
    Proc. Natl. Acad. Sci. U.S.A. 104:12685-12690(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND GINS4, SUBUNIT, REGION.

Entry informationi

Entry nameiPSF2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y248
Secondary accession number(s): D3DUM5, Q6IAG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.