Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y248

- PSF2_HUMAN

UniProt

Q9Y248 - PSF2_HUMAN

Protein

DNA replication complex GINS protein PSF2

Gene

GINS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. DNA strand elongation involved in DNA replication Source: Reactome
    2. mitotic cell cycle Source: Reactome

    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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:24575. GINS2.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA145008313.

    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

    ArrayExpressiQ9Y248.
    BgeeiQ9Y248.
    CleanExiHS_GINS2.
    GenevestigatoriQ9Y248.

    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
    MCMBPQ9BTE32EBI-747491,EBI-749378

    Protein-protein interaction databases

    BioGridi119664. 18 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 – 108
    Beta strandi13 – 219
    Beta strandi26 – 283
    Beta strandi31 – 333
    Beta strandi42 – 454
    Helixi46 – 549
    Beta strandi57 – 604
    Helixi68 – 8013
    Beta strandi81 – 833
    Helixi92 – 10312
    Helixi104 – 1063
    Beta strandi107 – 1093
    Helixi110 – 13728
    Beta strandi141 – 1444
    Helixi150 – 17021
    Turni172 – 1743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000246603.
    HOVERGENiHBG044983.
    InParanoidiQ9Y248.
    KOiK10733.
    OMAiVPPEWME.
    OrthoDBiEOG7GQXXJ.
    PhylomeDBiQ9Y248.
    TreeFamiTF314359.

    Family and domain databases

    InterProiIPR021151. GINS_complex.
    IPR007257. GINS_Psf2.
    IPR016906. GINS_Psf2_subgr.
    [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

    MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI    50
    NLKQRQKCRL LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL 100
    NHASDNIPKA DEIRTLVKDM WDTRIAKLRV SADSFVRQQE AHAKLDNLTL 150
    MEINTSGTFL TQALNHMYKL RTNLQPLEST QSQDF 185
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi37999822.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10953.1.
    RefSeqi NP_057179.1. NM_016095.2.
    UniGenei Hs.433180.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E9X X-ray 2.30 B/F 1-185 [» ]
    2EHO X-ray 3.00 C/G/K 1-185 [» ]
    2Q9Q X-ray 2.36 A/E 1-185 [» ]
    ProteinModelPortali Q9Y248.
    SMRi Q9Y248. Positions 1-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119664. 18 interactions.
    DIPi DIP-29332N.
    IntActi Q9Y248. 3 interactions.
    MINTi MINT-1469655.
    STRINGi 9606.ENSP00000253462.

    PTM databases

    PhosphoSitei Q9Y248.

    Polymorphism databases

    DMDMi 37999822.

    Proteomic databases

    MaxQBi Q9Y248.
    PaxDbi Q9Y248.
    PRIDEi Q9Y248.

    Protocols and materials databases

    DNASUi 51659.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253462 ; ENSP00000253462 ; ENSG00000131153 .
    GeneIDi 51659.
    KEGGi hsa:51659.
    UCSCi uc002fja.3. human.

    Organism-specific databases

    CTDi 51659.
    GeneCardsi GC16M085709.
    HGNCi HGNC:24575. GINS2.
    HPAi HPA057285.
    MIMi 610609. gene.
    neXtProti NX_Q9Y248.
    PharmGKBi PA145008313.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5093.
    HOGENOMi HOG000246603.
    HOVERGENi HBG044983.
    InParanoidi Q9Y248.
    KOi K10733.
    OMAi VPPEWME.
    OrthoDBi EOG7GQXXJ.
    PhylomeDBi Q9Y248.
    TreeFami TF314359.

    Enzyme and pathway databases

    Reactomei REACT_6776. Unwinding of DNA.

    Miscellaneous databases

    ChiTaRSi GINS2. human.
    EvolutionaryTracei Q9Y248.
    GeneWikii GINS2.
    GenomeRNAii 51659.
    NextBioi 55634.
    PROi Q9Y248.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y248.
    Bgeei Q9Y248.
    CleanExi HS_GINS2.
    Genevestigatori Q9Y248.

    Family and domain databases

    InterProi IPR021151. GINS_complex.
    IPR007257. GINS_Psf2.
    IPR016906. GINS_Psf2_subgr.
    [Graphical view ]
    PANTHERi PTHR12772. PTHR12772. 1 hit.
    Pfami PF05916. Sld5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028998. GINS_Psf2_subgr. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 113 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