PSF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSF2_HUMAN
• UniProt AC: Q9Y248
• Protein Name: DNA replication complex GINS protein PSF2
• Gene Name: GINS2
• Organism: Homo sapiens (Human).
• Sequence Length: 185
• Subcellular Localization: Nucleus.
• Protein Description: 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..
• Protein Sequence: MDAAEVEFLAEKELVTIIPNFSLDKIYLIGGDLGPFNPGLPVEVPLWLAINLKQRQKCRLLPPEWMDVEKLEKMRDHERKEETFTPMPSPYYMELTKLLLNHASDNIPKADEIRTLVKDMWDTRIAKLRVSADSFVRQQEAHAKLDNLTLMEINTSGTFLTQALNHMYKLRTNLQPLESTQSQDF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDAAEVEF -------CCHHHHHH	7.74	19413330
70	Ubiquitination	PEWMDVEKLEKMRDH CHHCCHHHHHHHCCC	62.89	29967540
73	Ubiquitination	MDVEKLEKMRDHERK CCHHHHHHHCCCCHH	50.07	-
80	Ubiquitination	KMRDHERKEETFTPM HHCCCCHHHCCCCCC	57.84	21906983
97	Ubiquitination	PYYMELTKLLLNHAS HHHHHHHHHHHHHHH	50.16	21963094
104	Phosphorylation	KLLLNHASDNIPKAD HHHHHHHHCCCCCHH	24.52	-
109	Ubiquitination	HASDNIPKADEIRTL HHHCCCCCHHHHHHH	65.75	21906983
109	Sumoylation	HASDNIPKADEIRTL HHHCCCCCHHHHHHH	65.75	28112733
118	Ubiquitination	DEIRTLVKDMWDTRI HHHHHHHHHHHHHCH	45.00	21906983
127	Ubiquitination	MWDTRIAKLRVSADS HHHHCHHHEECCHHH	34.16	17623298
158	Phosphorylation	MEINTSGTFLTQALN EEECCCHHHHHHHHH	18.42	-
172	Phosphorylation	NHMYKLRTNLQPLES HHHHHHHHCCCCCCC	51.20	23403867
179	Phosphorylation	TNLQPLESTQSQDF- HCCCCCCCCCCCCC-	39.15	25463755
180	Phosphorylation	NLQPLESTQSQDF-- CCCCCCCCCCCCC--	23.90	17525332
182	Phosphorylation	QPLESTQSQDF---- CCCCCCCCCCC----	31.63	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
182	S	Phosphorylation	Kinase	ATR	Q13535	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSF2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PSF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SLD5_HUMAN	GINS4	physical	16189514
CHK2_HUMAN	CHEK2	physical	17525332
FANCF_HUMAN	FANCF	physical	21109493
PSF3_HUMAN	GINS3	physical	21705323
SLD5_HUMAN	GINS4	physical	21705323
SLD5_HUMAN	GINS4	physical	22939629
PSF3_HUMAN	GINS3	physical	22939629
IF4H_HUMAN	EIF4H	physical	22863883
FERM2_HUMAN	FERMT2	physical	22863883
SLD5_HUMAN	GINS4	physical	25416956
PSF1_HUMAN	GINS1	physical	26344197
SLD5_HUMAN	GINS4	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-182, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-182, AND MASS SPECTROMETRY.
PubMed: 19413330

"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-182, ANDMASS SPECTROMETRY.
PubMed: 17525332