Type |
Details |
Score |
Protein Domain |
Type: |
Family |
Description: |
Centrosomal protein of 95kDa is localised to the centrosome and the spindle pole []. Its function is not clear. It is phosphorylated upon DNA damage, probably by ATM or ATR [, ]. |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
821
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
719
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
904
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
833
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
734
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
862
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
812
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
262
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
688
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
280
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
435
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
433
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
514
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
576
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
715
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
562
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
280
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
840
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Trost M |
Year: |
2009 |
Journal: |
Immunity |
Title: |
The phagosomal proteome in interferon-gamma-activated macrophages. |
Volume: |
30 |
Issue: |
1 |
Pages: |
143-54 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sweet SM |
Year: |
2009 |
Journal: |
Mol Cell Proteomics |
Title: |
Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. |
Volume: |
8 |
Issue: |
5 |
Pages: |
904-12 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
158
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Centrosomal protein of 170kDa (Cep170) plays a role in microtubule organisation []. Human Cep170 is constantly expressed throughout the cell cycle but phosphorylated during mitosis. Cep170 is a substrate of Polo-like kinase 1 (Plk1) []. It is associated with the mature mother centriole. Upon DNA damage, it is phosphorylated probably by ATM or ATR [, , ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This is a domain of unknown function with homology to the CH domain. This domain can be found in CEP95CEP95 is localised to the centrosome and the spindle pole []. Its function is not clear. It is phosphorylated upon DNA damage, probably by ATM or ATR [, ]. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
476
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
447
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Zanivan S |
Year: |
2008 |
Journal: |
J Proteome Res |
Title: |
Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry. |
Volume: |
7 |
Issue: |
12 |
Pages: |
5314-26 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
221
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
235
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
180
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
181
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
257
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
235
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
142
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
129
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
163
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
270
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
47
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
94
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
120
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
387
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
108
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
53
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
156
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
322
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
179
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
758
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
261
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
585
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
687
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
44
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Chini CC |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
Human claspin is required for replication checkpoint control. |
Volume: |
278 |
Issue: |
32 |
Pages: |
30057-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kumagai A |
Year: |
2000 |
Journal: |
Mol Cell |
Title: |
Claspin, a novel protein required for the activation of Chk1 during a DNA replication checkpoint response in Xenopus egg extracts. |
Volume: |
6 |
Issue: |
4 |
Pages: |
839-49 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lin SY |
Year: |
2004 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation. |
Volume: |
101 |
Issue: |
17 |
Pages: |
6484-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Muñoz IM |
Year: |
2012 |
Journal: |
J Biol Chem |
Title: |
Family with sequence similarity 60A (FAM60A) protein is a cell cycle-fluctuating regulator of the SIN3-HDAC1 histone deacetylase complex. |
Volume: |
287 |
Issue: |
39 |
Pages: |
32346-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Smith KT |
Year: |
2012 |
Journal: |
Mol Cell Proteomics |
Title: |
Human family with sequence similarity 60 member A (FAM60A) protein: a new subunit of the Sin3 deacetylase complex. |
Volume: |
11 |
Issue: |
12 |
Pages: |
1815-28 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nikali K |
Year: |
2002 |
Journal: |
Gene |
Title: |
cDNA cloning, expression profile and genomic structure of a novel human transcript on chromosome 10q24, and its analyses as a candidate gene for infantile onset spinocerebellar ataxia. |
Volume: |
299 |
Issue: |
1-2 |
Pages: |
111-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gauci S |
Year: |
2009 |
Journal: |
Anal Chem |
Title: |
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. |
Volume: |
81 |
Issue: |
11 |
Pages: |
4493-501 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kovalenko OV |
Year: |
1997 |
Journal: |
Nucleic Acids Res |
Title: |
A novel nucleic acid-binding protein that interacts with human rad51 recombinase. |
Volume: |
25 |
Issue: |
24 |
Pages: |
4946-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kim JW |
Year: |
2010 |
Journal: |
Int J Oncol |
Title: |
Involvement of C12orf32 overexpression in breast carcinogenesis. |
Volume: |
37 |
Issue: |
4 |
Pages: |
861-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zou L |
Year: |
2003 |
Journal: |
Science |
Title: |
Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. |
Volume: |
300 |
Issue: |
5625 |
Pages: |
1542-8 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents the FAM178 family, whose members are metazoan proteins and include FAM178A and FAM178B. The human FAM178A protein has been shown to be widely expressed []and is phosphorylated upon DNA damage, probably by ATM (ataxia telangiectasia mutated) or ATR (ATM and Rad3-related) [, ].FAM178A, also known as SLF2 (SMC5-SMC6 complex localization factor 2), forms a complex with RAD18 and SLF1, and together they define a pathway that suppresses genome instability by recruiting the SMC5/6 cohesion complex to DNA lesions [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
SIN3-HDAC complex-associated factor (also known as FAM60A) is found in eukaryotes. It has been shown to be a subunit of the Sin3 deacetylase complex (Sin3/HDAC), important for the repression of genes involved in the TGF-beta signaling pathway [, ]. Human FAM60A protein has been shown to be up-regulated in squamous cell carcinoma (SCC), adenocarcinoma (AC), colon, ovary, rectum and stomach tumors. Human FAM60A is phosphorylated upon DNA damage, probably by ATM or ATR []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Claspin is an essential protein for the ATR-Chk1-dependent activation ofthe DNA replication checkpoint response in Xenopus and human cells [, ]. DNA damage induces the formation of a complex between Claspin and BRCA1, a second regulator of Chk1 activation. It is thought that ATR regulates Claspin phosphorylation in response to DNA damage and replication stress, resulting in recruitment and phosphorylation of BRCA1. BRCA1 and Claspin then function to activate Chk1 [].This entry represents both claspin and claspin homologues found mainly in Drosophila. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
RAD51-associated protein 1 may participate in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair []. It functionally cooperates with PALB2 in promoting of D-loop formation by RAD51 [, ]. It binds to single and double stranded DNA, and is capable of aggregating DNA []. It also binds RNA []. It is phosphorylated upon DNA damage, probably by ATM or ATR [, , ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents ubinuclein-2 (UBN2). It contains a conserved HIRA-binding domain, which directly interacts with the N-terminal WD repeats of HIRA []. UBN2 and UBN1 are believed to be the orthologs of Hpc2p, a subunit of the HIR complex (a nucleosome assembly complex involved in regulation of histone gene transcription) in budding yeast []. It is phosphorylated upon DNA damage, probably by ATM or ATR []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents Rad9, Rad1, Hus1-interacting nuclear orphan protein 1 (RHINO or RHNO1), which plays a role in DNA damage response (DDR) signalling upon genotoxic stresses such as ionizing radiation (IR) during the S phase []. RHNO1 is recruited to sites of DNA damage through interaction with the Rad9-Rad1-Hus1 (9-1-1) complex and ATR activator TopBP1. It plays a role in ATR-mediated activation of Chk1 driven by TopBP1 and 9-1-1 []. It is involved in mammary carcinogenesis []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The function of the ATR-ATRIP (ATR-interacting protein) protein kinase complex is crucial for the cellular response to replication stress and DNA damage. ATRIP is a regulatory partner of ATR. The binding of ATRIP to replication protein A-coated ssDNA at sites of DNA damage drives ATR activation and enables the ATR-ATRIP complex to stimulate phosphorylation of substrates, such as Rad17 or Chk1, and the initiation of checkpoint signalling []. ATRIP deacetylation by SIRT2 promotes ATR-ATRIP bindingto RPA-ssDNA []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Dephoure N |
Year: |
2008 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
A quantitative atlas of mitotic phosphorylation. |
Volume: |
105 |
Issue: |
31 |
Pages: |
10762-7 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|