PSF3_HUMAN - dbPTM
PSF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSF3_HUMAN
UniProt AC Q9BRX5
Protein Name DNA replication complex GINS protein PSF3
Gene Name GINS3
Organism Homo sapiens (Human).
Sequence Length 216
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 MSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETDNAVPQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHFYGFGSQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED
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 Orthologous
Protein Cluster
31UbiquitinationDILMSHEKLPVRTET
HHHHCCCCCCCCCCC
53.30-
63 (in isoform 2)Phosphorylation-22.2227174698
65UbiquitinationNAVPQGSKLELPLWL
CCCCCCCCCCHHHHH
53.45-
74UbiquitinationELPLWLAKGLFDNKR
CHHHHHHHCCCCCCC
54.71-
74 (in isoform 2)Phosphorylation-54.7127174698
75 (in isoform 2)Phosphorylation-26.4327174698
79 (in isoform 2)Phosphorylation-32.1927174698
80UbiquitinationAKGLFDNKRRILSVE
HHCCCCCCCEEEEEE
44.92-
80AcetylationAKGLFDNKRRILSVE
HHCCCCCCCEEEEEE
44.9225953088
802-HydroxyisobutyrylationAKGLFDNKRRILSVE
HHCCCCCCCEEEEEE
44.92-
83 (in isoform 2)Phosphorylation-3.7927174698
84 (in isoform 2)Phosphorylation-4.4427174698
90 (in isoform 1)Ubiquitination-67.6721890473
90UbiquitinationILSVELPKIYQEGWR
EEEEECCHHHHCCHH
67.6721890473
90AcetylationILSVELPKIYQEGWR
EEEEECCHHHHCCHH
67.6723954790
117PhosphorylationHKMGPHFYGFGSQLL
HHCCCCCCCCCCCCC
14.4426074081
121PhosphorylationPHFYGFGSQLLHFDS
CCCCCCCCCCCCCCC
18.5226074081
128PhosphorylationSQLLHFDSPENADIS
CCCCCCCCCCCCCCC
32.9226074081
181UbiquitinationGLFQTGQKGLNDFQC
HHHHCCCCCCCCCCH
67.71-
191UbiquitinationNDFQCWEKGQASQIT
CCCCHHHCCCCHHCC
31.64-
195PhosphorylationCWEKGQASQITASNL
HHHCCCCHHCCHHHH
17.7725159151
207UbiquitinationSNLVQNYKKRKFTDM
HHHHHHHHHCCCCCC
54.36-
207AcetylationSNLVQNYKKRKFTDM
HHHHHHHHHCCCCCC
54.3624469663
212PhosphorylationNYKKRKFTDMED---
HHHHCCCCCCCC---
37.1524719451
251 (in isoform 3)Phosphorylation-24719451

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

Oops, there are no upstream regulatory protein records of PSF3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSF3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PSF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLD5_HUMANGINS4physical
22939629
PSF2_HUMANGINS2physical
26186194
MCM7_HUMANMCM7physical
26186194
TIM_HUMANTIMELESSphysical
26186194
PSF1_HUMANGINS1physical
26186194
MCM2_HUMANMCM2physical
26186194
SLD5_HUMANGINS4physical
26186194
CLSPN_HUMANCLSPNphysical
26186194
TIPIN_HUMANTIPINphysical
26186194
PSF1_HUMANGINS1physical
26344197
PSF2_HUMANGINS2physical
26344197
SLD5_HUMANGINS4physical
26344197
PSF2_HUMANGINS2physical
28514442
SLD5_HUMANGINS4physical
28514442
PSF1_HUMANGINS1physical
28514442
CLSPN_HUMANCLSPNphysical
28514442
TIM_HUMANTIMELESSphysical
28514442
TIPIN_HUMANTIPINphysical
28514442
MCM7_HUMANMCM7physical
28514442
SSRP1_HUMANSSRP1physical
28514442

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.
Regulatory Network of PSF3_HUMAN

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Related Literatures of Post-Translational Modification

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