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Q14691 (PSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication complex GINS protein PSF1
Alternative name(s):
GINS complex subunit 1
Gene names
Name:GINS1
Synonyms:KIAA0186, PSF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. GINS1 is essential for function. Ref.9

Subunit structure

Component of the GINS complex which is a heterotetramer of GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS4. GINS complex interacts with DNA primase in vitro. Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus By similarity.

Induction

Significantly up-regulated in aggressive melanomas. Ref.4

Sequence similarities

Belongs to the GINS1/PSF1 family.

Mass spectrometry

Molecular mass is 98373±13 Da from positions 1 - 196. Determined by ESI. This is the measured mass for the GINS complex. Ref.7

Sequence caution

The sequence BAA11503.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196DNA replication complex GINS protein PSF1
PRO_0000219035

Natural variations

Natural variant971V → I. Ref.3
Corresponds to variant rs6076347 [ dbSNP | Ensembl ].
VAR_051606

Secondary structure

.............. 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14691 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2270B5CE6C43BFE5

FASTA19622,988
        10         20         30         40         50         60 
MFCEKAMELI RELHRAPEGQ LPAFNEDGLR QVLEEMKALY EQNQSDVNEA KSGGRSDLIP 

        70         80         90        100        110        120 
TIKFRHCSLL RNRRCTVAYL YDRLLRIRAL RWEYGSVLPN ALRFHMAAEE MEWFNNYKRS 

       130        140        150        160        170        180 
LATYMRSLGG DEGLDITQDM KPPKSLYIEV RCLKDYGEFE VDDGTSVLLK KNSQHFLPRW 

       190 
KCEQLIRQGV LEHILS 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT ILE-97.
Tissue: Skin.
[4]"Comprehensive expression profiling of tumor cell lines identifies molecular signatures of melanoma progression."
Ryu B., Kim D.S., Deluca A.M., Alani R.M.
PLoS ONE 2:E594-E594(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Molecular architecture of the human GINS complex."
Boskovic J., Coloma J., Aparicio T., Zhou M., Robinson C.V., Mendez J., Montoya G.
EMBO Rep. 8:678-684(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH GINS2; GINS3 AND GINS4, SUBUNIT, MASS SPECTROMETRY OF GINS COMPLEX.
[8]"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) OF 1-151 IN COMPLEX WITH GINS2; GINS3 AND GINS4, SUBUNIT.
[9]"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) OF 1-149 IN COMPLEX WITH GINS2; GINS3 AND GINS4, SUBUNIT.
[10]"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 GINS2; GINS3 AND GINS4, SUBUNIT, REGION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D80008 mRNA. Translation: BAA11503.2. Different initiation.
AL353812, AL031672 Genomic DNA. Translation: CAI13764.1.
AL031672, AL353812 Genomic DNA. Translation: CAI43019.1.
BC012542 mRNA. Translation: AAH12542.1.
RefSeqNP_066545.3. NM_021067.3.
UniGeneHs.658464.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9XX-ray2.30A/E1-149[»]
2EHOX-ray3.00B/F/J1-151[»]
2Q9QX-ray2.36C/G1-196[»]
ProteinModelPortalQ14691.
SMRQ14691. Positions 1-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115174. 5 interactions.
DIPDIP-29331N.
STRING9606.ENSP00000262460.

PTM databases

PhosphoSiteQ14691.

Polymorphism databases

DMDM6226339.

Proteomic databases

PaxDbQ14691.
PeptideAtlasQ14691.
PRIDEQ14691.

Protocols and materials databases

DNASU9837.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262460; ENSP00000262460; ENSG00000101003.
GeneID9837.
KEGGhsa:9837.
UCSCuc002wuv.1. human.

Organism-specific databases

CTD9837.
GeneCardsGC20P025389.
HGNCHGNC:28980. GINS1.
HPAHPA051185.
HPA054486.
MIM610608. gene.
neXtProtNX_Q14691.
PharmGKBPA145008291.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5230.
HOGENOMHOG000192102.
HOVERGENHBG053743.
InParanoidQ14691.
KOK10732.
OMALQRNKRC.
OrthoDBEOG7M6D8F.
PhylomeDBQ14691.
TreeFamTF312848.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ14691.
BgeeQ14691.
CleanExHS_GINS1.
GenevestigatorQ14691.

Family and domain databases

InterProIPR005339. GINS_Psf1.
[Graphical view]
PANTHERPTHR12914. PTHR12914. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGINS1. human.
EvolutionaryTraceQ14691.
GeneWikiGINS1.
GenomeRNAi9837.
NextBio37066.
PROQ14691.
SOURCESearch...

Entry information

Entry namePSF1_HUMAN
AccessionPrimary (citable) accession number: Q14691
Secondary accession number(s): Q9NQE2, Q9NQI7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM