UniProt ID | CNBP_HUMAN | |
---|---|---|
UniProt AC | P62633 | |
Protein Name | Cellular nucleic acid-binding protein | |
Gene Name | CNBP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 177 | |
Subcellular Localization | Cytoplasm. Endoplasmic reticulum. | |
Protein Description | Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression.. | |
Protein Sequence | MSSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGGFTSDRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSSNECFKC ------CCCCCCCCC | 41.70 | 22814378 | |
2 | Phosphorylation | ------MSSNECFKC ------CCCCCCCCC | 41.70 | 27251275 | |
3 | Phosphorylation | -----MSSNECFKCG -----CCCCCCCCCC | 35.04 | 24719451 | |
3 (in isoform 6) | Phosphorylation | - | 35.04 | 24719451 | |
8 | Methylation | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | 83040663 | |
8 | Acetylation | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | - | |
8 | Ubiquitination | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | - | |
8 | Succinylation | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | 23954790 | |
8 | Acetylation | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | 23749302 | |
8 | Ubiquitination | MSSNECFKCGRSGHW CCCCCCCCCCCCCCC | 47.65 | - | |
11 | Methylation | NECFKCGRSGHWARE CCCCCCCCCCCCCCC | 49.27 | 115920677 | |
12 (in isoform 6) | Phosphorylation | - | 21.94 | 24719451 | |
12 | Phosphorylation | ECFKCGRSGHWAREC CCCCCCCCCCCCCCC | 21.94 | 26657352 | |
25 | Dimethylation | ECPTGGGRGRGMRSR CCCCCCCCCCCCCCC | 34.60 | - | |
25 | Methylation | ECPTGGGRGRGMRSR CCCCCCCCCCCCCCC | 34.60 | 24726729 | |
27 | Methylation | PTGGGRGRGMRSRGR CCCCCCCCCCCCCCC | 34.08 | 24726729 | |
27 | Dimethylation | PTGGGRGRGMRSRGR CCCCCCCCCCCCCCC | 34.08 | - | |
30 | Methylation | GGRGRGMRSRGRGGF CCCCCCCCCCCCCCC | 26.48 | 54560907 | |
32 (in isoform 5) | Methylation | - | 28.59 | 24129315 | |
32 (in isoform 2) | Methylation | - | 28.59 | 24129315 | |
32 (in isoform 8) | Methylation | - | 28.59 | 24129315 | |
32 | Dimethylation | RGRGMRSRGRGGFTS CCCCCCCCCCCCCCC | 28.59 | - | |
32 | Methylation | RGRGMRSRGRGGFTS CCCCCCCCCCCCCCC | 28.59 | 24394347 | |
34 (in isoform 5) | Methylation | - | 40.74 | 24129315 | |
34 (in isoform 2) | Methylation | - | 40.74 | 24129315 | |
34 | Dimethylation | RGMRSRGRGGFTSDR CCCCCCCCCCCCCHH | 40.74 | - | |
34 | Methylation | RGMRSRGRGGFTSDR CCCCCCCCCCCCCHH | 40.74 | 12018949 | |
34 (in isoform 8) | Methylation | - | 40.74 | 24129315 | |
41 (in isoform 8) | Phosphorylation | - | 47.82 | 29116813 | |
41 (in isoform 2) | Phosphorylation | - | 47.82 | 29116813 | |
41 (in isoform 5) | Phosphorylation | - | 47.82 | 29116813 | |
47 | Phosphorylation | DRGFQFVSSSLPDIC HHCCHHHHCCCCHHH | 18.59 | 22617229 | |
47 (in isoform 6) | Phosphorylation | - | 18.59 | 27251275 | |
48 | Acetylation | RGFQFVSSSLPDICY HCCHHHHCCCCHHHH | 30.50 | - | |
48 | Phosphorylation | RGFQFVSSSLPDICY HCCHHHHCCCCHHHH | 30.50 | 28348404 | |
48 | Ubiquitination | RGFQFVSSSLPDICY HCCHHHHCCCCHHHH | 30.50 | - | |
48 (in isoform 6) | Phosphorylation | - | 30.50 | 27251275 | |
49 | Phosphorylation | GFQFVSSSLPDICYR CCHHHHCCCCHHHHH | 36.09 | 22617229 | |
49 (in isoform 6) | Phosphorylation | - | 36.09 | 24719451 | |
54 | Glutathionylation | SSSLPDICYRCGESG HCCCCHHHHHCCCCC | 1.98 | 22555962 | |
55 | Phosphorylation | SSLPDICYRCGESGH CCCCHHHHHCCCCCC | 14.85 | 20068231 | |
65 | Ubiquitination | GESGHLAKDCDLQED CCCCCCCCCCCCCCC | 66.31 | - | |
65 | Acetylation | GESGHLAKDCDLQED CCCCCCCCCCCCCCC | 66.31 | 23749302 | |
68 | Acetylation | GHLAKDCDLQEDACY CCCCCCCCCCCCCCH | 62.61 | - | |
73 (in isoform 8) | Methylation | - | 9.28 | 24129315 | |
75 | Phosphorylation | DLQEDACYNCGRGGH CCCCCCCHHCCCCCC | 18.40 | 28796482 | |
79 | Methylation | DACYNCGRGGHIAKD CCCHHCCCCCCHHCC | 50.55 | 24129315 | |
80 (in isoform 4) | Methylation | - | 19.81 | 24129315 | |
85 | Acetylation | GRGGHIAKDCKEPKR CCCCCHHCCCCCCCH | 64.16 | 23749302 | |
86 | Ubiquitination | RGGHIAKDCKEPKRE CCCCHHCCCCCCCHH | 39.43 | - | |
86 | Acetylation | RGGHIAKDCKEPKRE CCCCHHCCCCCCCHH | 39.43 | - | |
97 | Acetylation | PKREREQCCYNCGKP CCHHHHHHHHHCCCC | 1.97 | 19608861 | |
97 | Ubiquitination | PKREREQCCYNCGKP CCHHHHHHHHHCCCC | 1.97 | 19608861 | |
97 | Glutathionylation | PKREREQCCYNCGKP CCHHHHHHHHHCCCC | 1.97 | 22555962 | |
98 | Acetylation | KREREQCCYNCGKPG CHHHHHHHHHCCCCC | 2.46 | 19608861 | |
98 | Ubiquitination | KREREQCCYNCGKPG CHHHHHHHHHCCCCC | 2.46 | 19608861 | |
99 | Phosphorylation | REREQCCYNCGKPGH HHHHHHHHHCCCCCC | 22.55 | 21945579 | |
101 | Ubiquitination | REQCCYNCGKPGHLA HHHHHHHCCCCCCHH | 2.75 | - | |
103 | Ubiquitination | QCCYNCGKPGHLARD HHHHHCCCCCCHHCC | 50.45 | - | |
103 | Acetylation | QCCYNCGKPGHLARD HHHHHCCCCCCHHCC | 50.45 | 23749302 | |
104 | Ubiquitination | CCYNCGKPGHLARDC HHHHCCCCCCHHCCC | 22.26 | 19608861 | |
104 | Acetylation | CCYNCGKPGHLARDC HHHHCCCCCCHHCCC | 22.26 | 19608861 | |
105 | Acetylation | CYNCGKPGHLARDCD HHHCCCCCCHHCCCC | 31.74 | 19608861 | |
105 | Ubiquitination | CYNCGKPGHLARDCD HHHCCCCCCHHCCCC | 31.74 | 19608861 | |
113 | Ubiquitination | HLARDCDHADEQKCY CHHCCCCCCCCHHCC | 41.22 | - | |
117 | Ubiquitination | DCDHADEQKCYSCGE CCCCCCCHHCCCCCC | 41.49 | - | |
118 | Acetylation | CDHADEQKCYSCGEF CCCCCCHHCCCCCCC | 32.85 | 25953088 | |
118 | Ubiquitination | CDHADEQKCYSCGEF CCCCCCHHCCCCCCC | 32.85 | - | |
119 | Glutathionylation | DHADEQKCYSCGEFG CCCCCHHCCCCCCCC | 2.78 | 22555962 | |
120 | Phosphorylation | HADEQKCYSCGEFGH CCCCHHCCCCCCCCC | 17.65 | 25394399 | |
121 | Phosphorylation | ADEQKCYSCGEFGHI CCCHHCCCCCCCCCC | 25.72 | 28348404 | |
123 (in isoform 6) | Phosphorylation | - | 27.59 | 27251275 | |
130 | Ubiquitination | GEFGHIQKDCTKVKC CCCCCCCCCCCEEEE | 54.92 | - | |
130 | Acetylation | GEFGHIQKDCTKVKC CCCCCCCCCCCEEEE | 54.92 | 25953088 | |
135 | Ubiquitination | IQKDCTKVKCYRCGE CCCCCCEEEEEECCC | 2.52 | - | |
143 | Phosphorylation | KCYRCGETGHVAINC EEEECCCCCCEEEEC | 20.19 | 23312004 | |
151 | Phosphorylation | GHVAINCSKTSEVNC CCEEEECCCCCCEEE | 34.18 | 20068231 | |
152 | Acetylation | HVAINCSKTSEVNCY CEEEECCCCCCEEEE | 59.27 | 25953088 | |
152 | Ubiquitination | HVAINCSKTSEVNCY CEEEECCCCCCEEEE | 59.27 | - | |
153 (in isoform 6) | Phosphorylation | - | 17.52 | 27251275 | |
153 | Phosphorylation | VAINCSKTSEVNCYR EEEECCCCCCEEEEE | 17.52 | 21945579 | |
154 | Phosphorylation | AINCSKTSEVNCYRC EEECCCCCCEEEEEC | 43.19 | 21945579 | |
159 | Phosphorylation | KTSEVNCYRCGESGH CCCCEEEEECCCCCC | 12.07 | 21945579 | |
164 | Phosphorylation | NCYRCGESGHLAREC EEEECCCCCCEEEEE | 19.45 | 21945579 | |
166 (in isoform 6) | Phosphorylation | - | 26.12 | 24719451 | |
172 | Phosphorylation | GHLARECTIEATA-- CCEEEEEEEEECC-- | 19.66 | 26437602 | |
174 (in isoform 6) | Phosphorylation | - | 23.09 | 24719451 | |
176 | Phosphorylation | RECTIEATA------ EEEEEEECC------ | 21.80 | 27251275 | |
178 (in isoform 6) | Phosphorylation | - | 24719451 |
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 CNBP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CNBP_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 CNBP_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
602668 | Dystrophia myotonica 2 (DM2) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY. |