UniProt ID | CGBP1_HUMAN | |
---|---|---|
UniProt AC | Q9UFW8 | |
Protein Name | CGG triplet repeat-binding protein 1 | |
Gene Name | CGGBP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 167 | |
Subcellular Localization | Nucleus . | |
Protein Description | Binds to nonmethylated 5'-d(CGG)(n)-3' trinucleotide repeats in the FMR1 promoter. May play a role in regulating FMR1 promoter.. | |
Protein Sequence | MERFVVTAPPARNRSKTALYVTPLDRVTEFGGELHEDGGKLFCTSCNVVLNHVRKSAISDHLKSKTHTKRKAEFEEQNVRKKQRPLTASLQCNSTAQTEKVSVIQDFVKMCLEANIPLEKADHPAVRAFLSRHVKNGGSIPKSDQLRRAYLPDGYENENQLLNSQDC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
15 | Phosphorylation | APPARNRSKTALYVT CCCCCCCCCCEEEEE | 37.60 | 23401153 | |
16 | Ubiquitination | PPARNRSKTALYVTP CCCCCCCCCEEEEEC | 34.28 | 24816145 | |
17 | Phosphorylation | PARNRSKTALYVTPL CCCCCCCCEEEEECH | 24.12 | 26074081 | |
20 | Phosphorylation | NRSKTALYVTPLDRV CCCCCEEEEECHHHH | 10.38 | 28796482 | |
22 | Phosphorylation | SKTALYVTPLDRVTE CCCEEEEECHHHHHC | 12.46 | 29978859 | |
26 | Methylation | LYVTPLDRVTEFGGE EEEECHHHHHCCCCE | 44.96 | - | |
40 | Ubiquitination | ELHEDGGKLFCTSCN EEECCCCEEEEEECH | 43.87 | 29967540 | |
56 | Phosphorylation | VLNHVRKSAISDHLK HHHHHHHHHHHHHHH | 21.92 | 25159151 | |
59 | Phosphorylation | HVRKSAISDHLKSKT HHHHHHHHHHHHCCC | 20.77 | 26270265 | |
71 | Acetylation | SKTHTKRKAEFEEQN CCCCCHHHHHHHHHH | 54.55 | 20167786 | |
82 | Ubiquitination | EEQNVRKKQRPLTAS HHHHHHHHCCCCCEE | 40.76 | 29967540 | |
89 | Phosphorylation | KQRPLTASLQCNSTA HCCCCCEEEECCCCC | 17.46 | 28555341 | |
111 | Glutathionylation | IQDFVKMCLEANIPL HHHHHHHHHHCCCCH | 2.29 | 22555962 | |
120 | Ubiquitination | EANIPLEKADHPAVR HCCCCHHHCCCHHHH | 67.79 | 29967540 | |
131 | Phosphorylation | PAVRAFLSRHVKNGG HHHHHHHHHHHHCCC | 17.56 | 24719451 | |
139 | Phosphorylation | RHVKNGGSIPKSDQL HHHHCCCCCCCHHHH | 36.80 | 24719451 | |
143 | Phosphorylation | NGGSIPKSDQLRRAY CCCCCCCHHHHHHHH | 25.82 | 24719451 | |
150 | Phosphorylation | SDQLRRAYLPDGYEN HHHHHHHHCCCCCCC | 19.56 | 20068231 | |
155 | Phosphorylation | RAYLPDGYENENQLL HHHCCCCCCCHHHHC | 23.98 | 20068231 | |
164 | Phosphorylation | NENQLLNSQDC---- CHHHHCCCCCC---- | 27.62 | 17525332 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
164 | S | Phosphorylation | Kinase | ATR | Q13535 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CGBP1_HUMAN !! |
* 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 CGBP1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CGBP1_HUMAN | CGGBP1 | physical | 25416956 | |
GLRX3_HUMAN | GLRX3 | physical | 25416956 | |
F124A_HUMAN | FAM124A | physical | 25416956 | |
DDB1_HUMAN | DDB1 | physical | 26344197 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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 SER-164, AND MASSSPECTROMETRY. |