Q9Y248 (PSF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication complex GINS protein PSF2

Alternative name(s):
GINS complex subunit 2

Gene names

Name:	GINS2
Synonyms:	PSF2
ORF Names:	CGI-122, DC5, HSPC037

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.16
Subunit structure	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. Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the GINS2/PSF2 family.
Mass spectrometry	Molecular mass is 98373±13 Da from positions 1 - 185. Determined by ESI. This is the measured mass for the GINS complex. Ref.14

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHEK2	O96017	2	EBI-747491,EBI-1180783

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 185

185

DNA replication complex GINS protein PSF2

PRO_0000194813

Amino acid modifications

Modified residue

180

1

Phosphothreonine Ref.11

Modified residue

182

1

Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13

Secondary structure

1

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185

Helix Strand Turn

Details...

Helix

3 – 10

8

Beta strand

13 – 21

9

Beta strand

26 – 28

3

Beta strand

31 – 33

3

Beta strand

42 – 45

4

Helix

46 – 54

9

Beta strand

57 – 60

4

Helix

68 – 80

13

Beta strand

81 – 83

3

Helix

92 – 103

12

Helix

104 – 106

3

Beta strand

107 – 109

3

Helix

110 – 137

28

Beta strand

141 – 144

4

Helix

150 – 170

21

Turn

172 – 174

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y248 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 4F6A18B1ED76F93C	FASTA	185	21,428
	10 20 30 40 50 60 MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI NLKQRQKCRL 70 80 90 100 110 120 LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL NHASDNIPKA DEIRTLVKDM 130 140 150 160 170 180 WDTRIAKLRV SADSFVRQQE AHAKLDNLTL MEINTSGTFL TQALNHMYKL RTNLQPLEST QSQDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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, MASS SPECTROMETRY.
[14]	"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 PSF1; PSF3 AND GINS4, SUBUNIT, MASS SPECTROMETRY OF GINS COMPLEX.
[15]	"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.
[16]	"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.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00007146.

RefSeq

NP_057179.1. NM_016095.2.

UniGene

Hs.433180.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29332N.

IntAct

Q9Y248. 2 interactions.

MINT

MINT-1469655.

STRING

9606.ENSP00000253462.

PTM databases

PhosphoSite

Q9Y248.

Polymorphism databases

DMDM

37999822.

Proteomic databases

PaxDb

Q9Y248.

PRIDE

Q9Y248.

Protocols and materials databases

DNASU

51659.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000253462; ENSP00000253462; ENSG00000131153.

GeneID

51659.

KEGG

hsa:51659.

UCSC

uc002fja.3. human.

Organism-specific databases

CTD

51659.

GeneCards

GC16M085709.

HGNC

HGNC:24575. GINS2.

MIM

610609. gene.

neXtProt

NX_Q9Y248.

PharmGKB

PA145008313.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5093.

HOGENOM

HOG000246603.

HOVERGEN

HBG044983.

InParanoid

Q9Y248.

KO

K10733.

OMA

VGPFRAG.

OrthoDB

EOG4WSWBN.

PhylomeDB

Q9Y248.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_383. DNA Replication.

Gene expression databases

Bgee

Q9Y248.

CleanEx

HS_GINS2.

Genevestigator

Q9Y248.

GermOnline

ENSG00000131153. Homo sapiens.

Family and domain databases

InterPro

IPR021151. GINS_complex.
IPR007257. GINS_Psf2.
IPR016906. GINS_Psf2_subgr.
[Graphical view]

PANTHER

PTHR12772. PTHR12772. 1 hit.

Pfam

PF05916. Sld5. 1 hit.
[Graphical view]

PIRSF

PIRSF028998. GINS_Psf2_subgr. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

GINS2. human.

EvolutionaryTrace

Q9Y248.

GenomeRNAi

51659.

NextBio

55634.

SOURCE

Search...

Entry information

Entry name

PSF2_HUMAN

Accession

Primary (citable) accession number: Q9Y248
Secondary accession number(s): D3DUM5, Q6IAG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.